臺灣博碩士論文加值系統

抗生素所產生的抗藥性是對未來健康福祉的嚴重障礙。頻繁使用抗生素是病原菌產生抗藥性菌株重要的原因之一。革蘭氏陰性的胃幽門螺桿菌 Helicobacter pylori (H. pylori)多重抗藥性菌株multidrug-resistant (MDR)是造成全球健康問題的主因之一。幽門桿菌的感染是十分普遍的，它與各種胃部疾病，包括胃炎，消化性潰瘍，和胃癌有很大的關係。目前治療幽門桿菌的方案(使用蛋白質幫浦抑制劑輔以三重或四重廣效性抗生素)是最理想的，但帶有高度的失敗率。在這樣發展下去有效的抗生素將面臨不足以對抗的境地，因此有必要發展對幽門桿菌新的抗菌手段。最有潛力之一的選擇就是抗菌胜肽Antimicrobial peptides (AMPs)，它是一種存在於脊椎與無脊椎動物之中具有攻防兼備能力的細胞溶解胜肽。它們可以迅速殺死各種微生物並具備額外的活性影響先天免疫以及發炎反應。另外對於細菌對常規抗生素的抗藥性也使得抗菌胜肽有機會成為新一代的抗生素。因此它們分子作用機制是相當吸引人並且需要去闡明的。在這裡我們描述兩種新的抗菌胜肽，名為Tilapia Piscidin4 (TP4) 以及 Epinecidin-1 (Epi-1)，這是我們篩選出具有生長抑制以及殺菌效果用來抵抗ATCC 43504﹑51653﹑700392 以及臨床分離具有抗生素抗藥性菌株CI-HC-028 (這些菌株為 CagA+﹑VacA+) 等幽門桿菌。TP4 與Epi-1 展現出最小抑菌濃度lowest minimum inhibitory concentrations (MIC)並顯示與抗生素一起時的協同作用。我們刺激sub-MIC以及體內傳遞抵抗試驗表明TP4 與Epi-1具有獨立對抗這些細菌的效果。這些抗菌胜肽製造孔洞破壞細菌細胞膜，在這裡我們提出一個體外膜滲透機制：在幽門桿菌上TP4會經由膜形成微膠粒，Epi-1則是使膜以馬鞍形的弧度張開。這些TP4 與Epi-1的行動模式預測是藉由螢光探針1-N-phenylnaphthylamine (NPN)洩漏試驗證實，以測量幽門桿菌暴露在TP4 與Epi-1抗菌胜肽時所改變的表面膜電位差來驗證。更進一步則以transmission electron microscopic studies (TEM)直接觀察體外殺菌機制，結果證明是使膜去極化以及破壞胞質成分的組成。TP4 與Epi-1在體內的的影響以及在感染幽門桿菌時選擇性的調節宿主系統免疫反應則是在小鼠模組上驗證。TP4 與Epi-1的免疫調控潛力是經由流式細胞儀篩選cytokines ﹑ T cell marker以及splenic subsets分析幽門桿菌感染後的胃癌相關基因表現。經由胃組織的colonization，幽門桿菌具備高度的Regulatory T (Tregs) subsets以及低Th17/Treg比例，並且同時表現前以及抗發炎的cytokines。TP4 與Epi-1選擇性的抑制Treg subset的數量，而且TP4顯著的恢復了Th17/Treg的比例。TP4 與Epi-1甚至向下調控前以及抗發炎的cytokines以及Foxp3轉錄因子在胃部組織的表現。誘導CD4+-Foxp3 Tregs的損耗是因為幽門桿菌在早期被清除; 此外TP4 與Epi-1處理會經由抑制Th17 subsets幫助胃部恢復正常型態。小鼠與兔子的細胞毒性研究(口服﹑皮膚/真皮和眼睛的刺激測試)證實了TP4 與Epi-1的安全性，高劑量的胜肽並未造成在口服﹑真皮和眼睛的刺激測試產生毒性影響。總而言之，我們的結果顯示TP4 與Epi-1清除幽門桿菌是藉由一獨特的模式，在體外以膜溶解以及在體內強力影響調停幽門桿菌誘導宿主反應。高濃度的TP4 與Epi-1並不會造成小鼠與兔子的異常。因此，這兩種抗菌胜肽可以被視為對抗多重抗藥性幽門桿菌感染具有療效的新型藥劑。

The ongoing development of antibiotic-resistant infections is a major obstacle in ensuring future health and wellbeing. The frequent misuse of antibiotics is one of the reasons behind the development of resistance in pathogenic strains of bacteria. Emergence of multidrug-resistant (MDR) strains of the Gram-negative gastric pathogen Helicobacter pylori (H. pylori) is a global health concern. H. pylori infection is highly prevalent, and has a strong association with various gastric diseases, including gastritis, digestive ulcers, and gastric cancer. Currently, treatment of H. pylori infection (involving the use of proton pump inhibitors followed by triple and quadruple therapy with broad-spectrum antibiotics) is suboptimal, with high failure rates. This development is predicted to result in imminent inadequacy of applicable effective antibiotics, necessitating the development of novel antimicrobial strategies against H. pylori. Among the potential alternatives are antimicrobial peptides (AMPs), which are cytolytic peptides that serve in vertebrates and invertebrates for both offensive and defensive purposes. They can rapidly kill a broad range of microbes, and have additional activities that impact on the quality and effectiveness of innate responses and inflammation. Furthermore, the challenge of bacterial resistance to conventional antibiotics and the unique mode of action of AMPs have made such peptides promising candidates for the development of a new class of antibiotics. Accordingly, the molecular basis of their action is of considerable interest and needs to be elucidated. Here, we report our recent analyses of two novel AMPs, called Tilapia Piscidin 4 (TP4) and Epinecidin-1 (Epi-1), which we screened for growth inhibitory and/or bactericidal effects against H. pylori strains ATCC 43504, 51653, and 700392, and clinical isolate-antibiotic resistant strains CI-HC-028 (these strains are CagA+, VacA+). TP4 and Epi-1 displayed low minimum inhibitory concentrations (MIC) and synergistic activity with conventional antibiotics. Our simulated sub-MIC and in vivo passaging resistant assay showed that TP4 and Epi-1 efficacy is independent of resistance in bacteria. These AMPs create pores that cause bacterial membrane disruption, and here, we propose in vitro mechanisms of membrane permeabilization: TP4 acts via Membrane micelle formation, while Epi-1 acts via Saddle splay curvature generation. These modes of action of TP4 and Epi-1 were demonstrated using hydrophobic fluorescent probe 1-Nphenylnaphthylamine (NPN) leakage assay, and detection of changes in surface charge by measuring the zeta potential of H. pylori upon exposure to TP4 or Epi-1. Furthermore, transmission electron microscopic studies (TEM) were performed to evidence the in vitro direct killing mechanism underlying the membrane depolarization and disruption of periplasmic constituents. The in vivo efficacy of TP4 and Epi-1, as well as selective modulation of H. pylori-biased host immune responses, were demonstrated in a mouse model. The immunomodulatory potentials of TP4 and Epi-1 were analyzed in the host during H. pylori infection based on gastric gene expression, and analysis of cytokines, cell markers, and splenic subsets by flow cytometry. During colonization of gastric tissue, H. pylori maintains high regulatory T (Tregs) subsets and a low Th17/Treg ratio, and express both pro- and anti-inflammatory cytokines. TP4 and Epi-1 selectively suppressed the Treg subset population, and TP4 significantly restored the Th17/Treg ratio. Furthermore, TP4 and Epi-1 down regulated gene expression for both pro- and antiinflammatory cytokines and Foxp3 transcription factor in gastric tissue. The induced depletion of CD4+-Foxp3 Tregs results in early clearance of H. pylori density; moreover, TP4 and Epi-1 treatment helped restore normal gastric morphology by moderate suppression of Th17 subsets. Mouse and rabbit toxicity studies (oral, skin/dermal, and eye irritation tests) were performed to evaluate the safety of TP4 and Epi-1; crucially, high doses of peptides did not exert toxic effects in oral, dermal, or eye irritation models. Collectively, our results indicate that TP4 and Epi-1 clear H. pylori colonization through unique modes of membrane lysis in vitro, and strong in vivo efficacy and modulation of H. pylori-induced host responses. High concentrations of TP4 and Epi-1 did not induce abnormalities in mice or rabbits. Therefore, both peptides may be considered promising and novel agents for the monotherapeutic treatment of multidrug resistant H. pylori infections.

CONTENTS
I. Abstract Chinese………..……………………………………………………………..…vi-vii English…………………………….…………………………………….……...viii-x
II. Abbreviations ……………………………………………………………..…..xiv-xv
CHAPTER I
A. HELICOBACTER PYLORI INFECTION AND ITS TREATMENT
1. Introduction.……………………………………………………………………..…1
1.1. Helicobacter pylori discovery and morphology……………………………….2-5
1.2. Virulence factors ……………………………………………………….….......6-7
1.2.1. Flagellae ………………………………………………………….………8
1.2.2. Adhesion proteins....………………………..…………………….….........9
1.2.3. VacA………………………………………………………………….10-11
1.2.4. CagA....…………………………………………………………….....12-13
1.2.5. Urease B ...…………………………………………………………...14-16
1.2.6. Lipopolysaccharides (LPS) ……………………………….……….…17-19
1.3. H. pylori and Host Immune Responses...…………………………………...20-22
1.4. Clinical aspects of H. pylori-associated diseases………………...……..…...23-25
1.5. Antibiotic therapy and its failure ……………………………………….…...26-28



B. POST ANTIBIOTIC ERA: ANTIMICROBIAL PEPTIDES
2. Background ……………………………………………………………………......29
2.1. AMPS: A diverse collection of biomolecules …………..…………………..30-32
2.2. AAMPs: Anionic antimicrobial peptides …………………….………..…....32-36
2.3. CAMPs: Cationic antimicrobial peptides ……….…………....………….........37
2.3.1. Anti-bacterial peptides……………………………………………..…37-38
2.3.2. Anti-fungal peptides ……………………………………………………..39
2.3.3. Anti-parasite peptides ……………………………………………..........40
2.4. Anti-viral peptides ……………………………………………...….………..40-41
2.5. Tools for delivery of antimicrobial peptides ……………………………....42-43
2.6. Commercialization and clinical development of antimicrobial peptides.….44-45
2.7. Specific aims of the present investigation ……………………………….…… 46

CHAPTER II
CATIONIC ANTIMICROBIAL PEPTIDE: TILAPIA PISCIDIN 4 (TP4)
3. Introduction.…………………………………………...…………….…………..47-51
3.1. Materials and Method.. ……………………………………..……………….52-61
3.2. Results.……………………………………………………..………………..62-75
3.3. Figures and tables ……………………..…………………..……………….76-90



CHAPTER III
CATIONIC ANTIMICROBIAL PEPTIDE: EPINECIDIN-1 (EPI-1)
4. Introduction …………………………………………...…………….………….91-93
4.1. Materials and Methods...…………..……………………………….………94-101
4.2. Results.………………………………………………………………...….102-109
4.3. Figures and tables..………………………………………………………..110-121

CHAPTER IV
DISCUSSION AND FUTURE PROSPECTS
5. Discussion….………………………………………………………………….122-129
6. Conclusion………………………………………………………………….…130-131
7. Future Prospects ....……………………………………………………………132-133
8. References………...………….………………………………………………..134-189

APPENDICES
1. List of Primers ...…………………………………………………………..190-191
2. Curriculum Vitae.………………………………………………………….192-193

Agarwal, A., Lvov, Y., Sawant, R., &; Torchilin, V. (2008). Stable nanocolloids of poorly soluble drugs with high drug content prepared using the combination of sonication and layer-by-layer technology. Journal of Controlled Release, 128(3), 255-260.
Agudo, S., Alarcon, T., Cibrelus, L., Urruzuno, P., Martinez, M. J., &; Lopez-Brea, M. (2009). High percentage of clarithromycin and metronidazole resistance in Helicobacter pylori clinical isolates obtained from Spanish children. Rev Esp Quimioter, 22(2), 88-92.
Aihara, E., Closson, C., Matthis, A. L., Schumacher, M. A., Engevik, A. C., Zavros, Y., Montrose, M. H. (2014). Motility and Chemotaxis Mediate the Preferential Colonization of Gastric Injury Sites by Helicobacter pylori. PLoS Pathog, 10(7), e1004275.
Akira, S., Takeda, K., &; Kaisho, T. (2001). Toll-like receptors: critical proteins linking innate and acquired immunity. Nat Immunol, 2(8), 675-680.
Altschuler, E. (1996). Gastric Helicobacter pylori infection as a cause of idiopathic parkinson disease and non-arteric anterior optic ischemic neuropathy. Medical Hypotheses, 47(5), 413-414.
Alves, C. S., Melo, M. N., Franquelim, H. G., Ferre, R., Planas, M., Feliu, L., .Castanho, M. A. (2010). Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR. J Biol Chem, 285(36), 27536-27544.
Amedei, A., Cappon, A., Codolo, G., Cabrelle, A., Polenghi, A., Benagiano, M., de Bernard, M. (2006). The neutrophil-activating protein of Helicobacter pylori promotes Th1 immune responses. J Clin Invest, 116(4), 1092-1101.
Aoki, W., &; Ueda, M. (2013). Characterization of Antimicrobial Peptides toward the Development of Novel Antibiotics. Pharmaceuticals (Basel), 6(8), 1055-1081.
Appelmelk, B. J., Martin, S. L., Monteiro, M. A., Clayton, C. A., McColm, A. A., Zheng, P.,Kusters, J. G. (1999). Phase Variation in Helicobacter pyloriLipopolysaccharide due to Changes in the Lengths of Poly(C) Tracts in α3-Fucosyltransferase Genes. Infect Immun, 67(10), 5361-5366.
Arias, C. A., &; Murray, B. E. (2009a). Antibiotic-resistant bugs in the 21st century a clinical super-challenge. 360. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/19179312 (5)
Arias, C. A., &; Murray, B. E. (2009b). Antibiotic-resistant bugs in the 21st century a clinical super-challenge. N Engl J Med, 360(5), 439-443.
Armstrong, J. A., Wee, S. H., Goodwin, C. S., &; Wilson, D. H. (1987). Response of Campylobacter pyloridis to antibiotics, bismuth and an acid-reducing agent in vitro—an ultrastructural study. Journal of Medical Microbiology, 24(4), 343-350.
Balkovec, J. M., Hughes, D. L., Masurekar, P. S., Sable, C. A., Schwartz, R. E., &; Singh, S. B. (2014). Discovery and development of first in class antifungal caspofungin Natural Product Reports, 31(1), 15-34.
Ballam, L. D., Mendall, M. A., Asante, M., Morris, J., Strachan, D. P., Whincup, P. H., &; Cook, D. G. (2000). Western blotting is useful in the salivary diagnosis of Helicobacter pylori infection. Journal of Clinical Pathology, 53(4), 314-317.
Ballweber, L. M., Jaynes, J. E., Stamm, W. E., &; Lampe, M. F. (2002). In vitro microbicidal activities of cecropin peptides D2A21 and D4E1 and gel formulations containing 0.1 to 2% D2A21 against Chlamydia trachomatis. Antimicrob Agents Chemother, 46(1), 34-41.
Bastian, A., &; Schäfer, H. (2001). Human α-defensin 1 (HNP-1) inhibits adenoviral infection in vitro. Regulatory Peptides, 101(1–3), 157-161.
Bergese, S. D., Candiotti, K. A., Bokesch, P. M., Zura, A., Wisemandle, W., &; Bekker, A. Y. (2010). A Phase IIIb, randomized, double-blind, placebo-controlled, multicenter study evaluating the safety and efficacy of dexmedetomidine for sedation during awake fiberoptic intubation. Am J Ther, 17(6), 586-595.
Bergman, M. P., Engering, A., Smits, H. H., van Vliet, S. J., van Bodegraven, A. A., Wirth, H.-P., Appelmelk, B. J. (2004). Helicobacter pylori Modulates the T Helper Cell 1/T Helper Cell 2 Balance through Phase-variable Interaction between Lipopolysaccharide and DC-SIGN. The Journal of Experimental Medicine, 200(8), 979-990.
Bergman, M., Del Prete, G., van Kooyk, Y., &; Appelmelk, B. (2006). Helicobacter pylori phase variation, immune modulation and gastric autoimmunity. Nat Rev Micro, 4(2), 151-159.
Berry, V., Jennings, K., &; Woodnutt, G. (1995). Bactericidal and morphological effects of amoxicillin on Helicobacter pylori. Antimicrobial Agents and Chemotherapy, 39(8), 1859-1861.
Blaser, M. J. (1987). Gastric Campylobacter-like organisms, gastritis, and peptic ulcer disease. Gastroenterology, 93(2), 371-383.
Bode, G., Mauch, F., &; Malfertheiner, P. (1993). The Coccoid Forms of Helicobacter pylori. Criteria for Their Viability. Epidemiology and Infection, 111(3), 483-490.
Boman, H. G. (1995). Peptide Antibiotics and their Role in Innate Immunity. Annual Review of Immunology, 13(1), 61-92.
Borody, T. J., Cole, P., Noonan, S., Morgan, A., Lenne, J., Hyland, L., George, L. L. (1989). Recurrence of duodenal ulcer and Campylobacter pylori infection after eradication. Medical Journal of Australia, 151(8), 431-435.
Boughan, P. K., Argent, R. H., Body-Malapel, M., Park, J. H., Ewings, K. E., Bowie, A. G., Bajaj-Elliott, M. (2006). Nucleotide-binding oligomerization domain-1 and epidermal growth factor receptor: critical regulators of beta-defensins during Helicobacter pylori infection. J Biol Chem, 281(17), 11637-11648.
Braden, B., Teuber, G., Dietrich, C. F., Caspary, W. F., &; Lembcke, B. (2000). Comparison of new faecal antigen test with (13)C-urea breath test for detecting Helicobacter pylori infection and monitoring eradication treatment: prospective clinical evaluation. BMJ : British Medical Journal, 320(7228), 148-148.
Brogden, K. A. (2005). Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat Rev Microbiol, 3(3), 238-250.
Brogden, N. K., &; Brogden, K. A. (2011). Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals? International Journal of Antimicrobial Agents, 38(3), 217-225.
Castillo-Rojas, G., Mazari-Hiriart, M., &; Lopez-Vidal, Y. (2004). Helicobacter pylori: focus on CagA and VacA major virulence factors. Salud Publica Mex, 46(6), 538-548.
Censini, S., Lange, C., Xiang, Z., Crabtree, J. E., Ghiara, P., Borodovsky, M., Covacci, A. (1996). cag, a pathogenicity island of Helicobacter pylori, encodes type I-specific and disease-associated virulence factors. Proc Natl Acad Sci U S A, 93(25), 14648-14653.
Chan, D. I., Prenner, E. J., &; Vogel, H. J. (2006). Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1758(9), 1184-1202.
Chen, S. A., Slavin, M., &; Sorrell, T. (2011). Echinocandin Antifungal Drugs in Fungal Infections. Drugs, 71(1), 11-41.
Chen, X. Y., Liu, W. Z., Shi, Y., Zhang, D. Z., Xiao, S. D., &; Tytgat, G. N. J. (2002). Helicobacter pylori associated gastric diseases and lymphoid tissue hyperplasia in gastric antral mucosa. Journal of Clinical Pathology, 55(2), 133-137.
Chen, X. Y., Liu, W. Z., Shi, Y., Zhang, D. Z., Xiao, S. D., &; Tytgat, G. N. J. (2002). Helicobacter pylori associated gastric diseases and lymphoid tissue hyperplasia in gastric antral mucosa. Journal of Clinical Pathology, 55(2), 133-137.
Chey, W. D., &; Wong, B. C. (2007). American College of Gastroenterology guideline on the management of Helicobacter pylori infection. American Journal of Gastroenterology, 102(8), 1808-1825.
Chow, W.-H., Blaser, M. J., Blot, W. J., Gammon, M. D., Vaughan, T. L., Risch, H. A., Fraumeni, J. F. (1998). An Inverse Relation between cagA+ Strains of Helicobacter pylori Infection and Risk of Esophageal and Gastric Cardia Adenocarcinoma. Cancer Research, 58(4), 588-590.
Chuah, S.-K., Tsay, F.-W., Hsu, P.-I., &; Wu, D.-C. (2011). A new look at anti-Helicobacter pylori therapy. World J Gastroenterol, 17(35), 3971-3975.
Cirioni, O., Silvestri, C., Ghiselli, R., Kamysz, W., Minardi, D., Castelli, P., Giacometti, A. (2013). In vitro and in vivo effects of sub-MICs of pexiganan and imipenem on Pseudomonas aeruginosa adhesion and biofilm development. Infez Med, 21(4), 287-295.
Colovai, A. I., Giatzikis, C., Ho, E. K., Farooqi, M., Suciu-Foca, N., Cattoretti, G., &; Orazi, A. (2004). Flow cytometric analysis of normal and reactive spleen. Mod Pathol, 17(8), 918-927.
Conlon, J. M. (2008). Reflections on a systematic nomenclature for antimicrobial peptides from the skins of frogs of the family Ranidae. Peptides, 29(10), 1815-1819.
Correa, P., &; Houghton, J. (2007). Carcinogenesis of Helicobacter pylori. Gastroenterology, 133(2), 659-672.

Correa, P., &; Piazuelo, M. B. (2011). Helicobacter pylori Infection and Gastric Adenocarcinoma. US gastroenterology &; hepatology review, 7(1), 59-64.
Costa, F., Maia, S., Gomes, J., Gomes, P., &; Martins, M. C. (2014). Characterization of hLF1-11 immobilization onto chitosan ultrathin films, and its effects on antimicrobial activity. Acta Biomater, 10(8), 3513-3521.
Coudron, P. E., &; Stratton, C. W. (1995). Utilization of time-kill kinetic methodologies for assessing the bactericidal activities of ampicillin and bismuth, alone and in combination, against Helicobacter pylori in stationary and logarithmic growth phases. Antimicrob Agents Chemother, 39(1), 66-69.
Covacci, A., Censini, S., Bugnoli, M., Petracca, R., Burroni, D., Macchia, G., et al. (1993). Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer. Proc Natl Acad Sci U S A, 90(12), 5791-5795.
Covacci, A., Telford, J. L., Giudice, G. D., Parsonnet, J., &; Rappuoli, R. (1999). Helicobacter pylori Virulence and Genetic Geography. Science, 284(5418), 1328-1333.
Crabtree, J. E. (2000). Book Review. New England Journal of Medicine, 342(11), 827-828.
Crabtree, J. E., Peichl, P., Wyatt, J. I., Stachl, U., &; Lindley, I. J. (1993). Gastric interleukin-8 and IgA IL-8 autoantibodies in Helicobacter pylori infection. Scand J Immunol, 37(1), 65-70.
Crabtree, J. E., Shallcross, T. M., Heatley, R. V., &; Wyatt, J. I. (1991). Mucosal tumour necrosis factor alpha and interleukin-6 in patients with Helicobacter pylori associated gastritis. Gut, 32(12), 1473-1477.
Crabtree, J. E., Taylor, J. D., Heatley, R. V., Shallcross, T. M., Rathbone, B. J., Wyatt, J. I., &; Tompkins, D. S. (1991). Mucosal IgA recognition of Helicobacter pylori 120 kDa protein, peptic ulceration, and gastric pathology. The Lancet, 338(8763), 332-335.
Cummins, J. E., Jr., Guarner, J., Flowers, L., Guenthner, P. C., Bartlett, J., Morken, T., Dezzutti, C. S. (2007). Preclinical testing of candidate topical microbicides for anti-human immunodeficiency virus type 1 activity and tissue toxicity in a human cervical explant culture. Antimicrob Agents Chemother, 51(5), 1770-1779.
Czajkowsky, D. M., Iwamoto, H., Cover, T. L., &; Shao, Z. (1999). The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH. Proc Natl Acad Sci U S A, 96(5), 2001-2006.
Dashper, S. G., O''Brien-Simpson, N. M., Cross, K. J., Paolini, R. A., Hoffmann, B., Catmull, D. V., Reynolds, E. C. (2005). Divalent Metal Cations Increase the Activity of the Antimicrobial Peptide Kappacin. Antimicrob Agents Chemother, 49(6), 2322-2328.
Dashper, S., Liu, S., &; Reynolds, E. (2007). Antimicrobial Peptides and their Potential as Oral Therapeutic Agents. International Journal of Peptide Research and Therapeutics, 13(4), 505-516.
de Almeida Vaucher, R., de Campos Velho Gewehr, C., Folmer Correa, A. P., Sant‘Anna, V., Ferreira, J., &; Brandelli, A. (2011). Evaluation of the immunogenicity and in vivo toxicity of the antimicrobial peptide P34. International Journal of Pharmaceutics, 421(1), 94-98.
de Bernard, M., Burroni, D., Papini, E., Rappuoli, R., Telford, J., &; Montecucco, C. (1998). Identification of the Helicobacter pylori VacA toxin domain active in the cell cytosol. Infect Immun, 66(12), 6014-6016.
de Korwin, J. D. (2008). [Does Helicobacter pylori infection play a role in extragastric diseases?]. Presse Med, 37(3 Pt 2), 525-534.
D''Elios, M. M., Manghetti, M., Almerigogna, F., Amedei, A., Costa, F., Burroni, D., Del Prete, G. (1997). Different cytokine profile and antigen-specificity repertoire in Helicobacter pylori-specific T cell clones from the antrum of chronic gastritis patients with or without peptic ulcer. Eur J Immunol, 27(7), 1751-1755.
Dezfuli, B. S., Lui, A., Giari, L., Pironi, F., Manera, M., Lorenzoni, M., &; Noga, E. J. (2013). Piscidins in the intestine of European perch, Perca fluviatilis, naturally infected with an enteric worm. Fish Shellfish Immunol, 35(5), 1539-1546.
Dobbs, R. J., Dobbs, S. M., Weller, C., Bjarnason, I. T., Oxlade, N. L., Charlett, A., Price, A. B. (2005). Role of Chronic Infection and Inflammation in the Gastrointestinal Tract in the Etiology and Pathogenesis of Idiopathic Parkinsonism. Helicobacter, 10(4), 267-275.
Domingues, M. M., Castanho, M. A. R. B., &; Santos, N. C. (2009). rBPI21 Promotes Lipopolysaccharide Aggregation and Exerts Its Antimicrobial Effects by (Hemi)fusion of PG-Containing Membranes. PLoS ONE, 4(12), e8385.
Domingues, M. M., Santiago, P. S., Castanho, M. A. R. B., &; Santos, N. C. (2008). What can light scattering spectroscopy do for membrane-active peptide studies? Journal of Peptide Science, 14(4), 394-400.
Domingues, M. M., Santos, N. C., &; Castanho, M. A. (2012). Antimicrobial peptide rBPI21: a translational overview from bench to clinical studies. Curr Protein Pept Sci, 13(7), 611-619.
Duncan, S. S., Valk, P. L., Shaffer, C. L., Bordenstein, S. R., &; Cover, T. L. (2012). J-Western Forms of Helicobacter pylori cagA Constitute a Distinct Phylogenetic Group with a Widespread Geographic Distribution. Journal of Bacteriology, 194(6), 1593-1604.
Dunn, B. E., &; Grutter, M. G. (2001). Helicobacter pylori springs another surprise. [10.1038/88527]. Nat Struct Mol Biol, 8(6), 480-482.
Dunn, B. E., Cohen, H., &; Blaser, M. J. (1997). Helicobacter pylori. Clinical Microbiology Reviews, 10(4), 720-741.
Duvic, B., Jouan, V., Essa, N., Girard, P. A., Pagès, S., Abi Khattar, Z., Escoubas, J. M. (2012). Cecropins as a marker of Spodoptera frugiperda immunosuppression during entomopathogenic bacterial challenge. Journal of Insect Physiology, 58(6), 881-888.
Eaton, K. A., Morgan, D. R., &; Krakowka, S. (1989). Campylobacter pylori virulence factors in gnotobiotic piglets. Infect Immun, 57(4), 1119-1125.
Eaton, K. A., Morgan, D. R., &; Krakowka, S. (1992). Motility as a factor in the colonisation of gnotobiotic piglets by Helicobacter pylori. J Med Microbiol, 37(2), 123-127.
Eaton, K. A., Suerbaum, S., Josenhans, C., &; Krakowka, S. (1996). Colonization of gnotobiotic piglets by Helicobacter pylori deficient in two flagellin genes. Infect Immun, 64(7), 2445-2448.
Eisenstein, E. M., &; Williams, C. B. (2009). The Treg/Th17 Cell Balance: A New Paradigm for Autoimmunity. Pediatr Res, 65(5 Part 2), 26R-31R.
Ellison, R. T., 3rd, Giehl, T. J., &; LaForce, F. M. (1988). Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infection and Immunity, 56(11), 2774-2781.
Ernst, P. B., &; Gold, B. D. (2000). The disease spectrum of Helicobacter pylori: the immunopathogenesis of gastroduodenal ulcer and gastric cancer.
Fiorentino, M., Ding, H., Blanchard, T. G., Czinn, S. J., Sztein, M. B., &; Fasano, A. (2013). Helicobacter pylori-Induced Disruption of Monolayer Permeability and Proinflammatory Cytokine Secretion in Polarized Human Gastric Epithelial Cells. Infect Immun, 81(3), 876-883.
Fischbach, L., &; Evans, E. L. (2007a). Meta-analysis: the effect of antibiotic resistance status on the efficacy of triple and quadruple first-line therapies for Helicobacter pylori. Alimentary Pharmacology &; Therapeutics, 26(3), 343-357.
Fischbach, L., &; Evans, E. L. (2007b). Meta-analysis: the effect of antibiotic resistance status on the efficacy of triple and quadruple first-line therapies for Helicobacter pylori. [Meta-Analysis]. Alimentary Pharmacology and Therapeutics, 26(3), 343-357.
Fock, K. M., Graham, D. Y., &; Malfertheiner, P. (2013). Helicobacter pylori research: historical insights and future directions. Nat Rev Gastroenterol Hepatol, 10(8), 495-500.
Fosgerau, K., &; Hoffmann, T. (2015). Peptide therapeutics: current status and future directions. [Review]. Drug Discov Today, 20(1), 122-128.
Fossiez, F., Djossou, O., Chomarat, P., Flores-Romo, L., Ait-Yahia, S., Maat, C., Lebecque, S. (1996). T cell interleukin-17 induces stromal cells to produce proinflammatory and hematopoietic cytokines. J Exp Med, 183(6), 2593-2603.
Fox, J. L. (2013). Antimicrobial peptides stage a comeback. [News]. Nat Biotech, 31(5), 379-382.
Franceschi, F., &; Gasbarrini, A. (2007). Helicobacter pylori and extragastric diseases. Best Pract Res Clin Gastroenterol, 21(2), 325-334.
Franceschi, F., Tortora, A., Gasbarrini, G., &; Gasbarrini, A. (2014). Helicobacter pylori and extragastric diseases. Helicobacter, 19 Suppl 1, 52-58.
Garner, J. A., &; Cover, T. L. (1996). Binding and internalization of the Helicobacter pylori vacuolating cytotoxin by epithelial cells. Infect Immun, 64(10), 4197-4203.
Gasbarrini, A., Carloni, E., Gasbarrini, G., &; Chisholm, S. A. (2004). Helicobacter pylori and extragastric diseases--other Helicobacters. Helicobacter, 9 Suppl 1, 57-66.
Gasbarrini, A., Carloni, E., Gasbarrini, G., &; Menard, A. (2003). Helicobacter pylori and extragastric diseases -- other helicobacters. Helicobacter, 8 Suppl 1, 68-76.
Gasbarrini, A., Fox, J., &; Gasbarrini, G. (2000). Helicobacter pylori and other Helicobacter spp. chronic infections and extragastric diseases. Eur J Gastroenterol Hepatol, 12(9), 1057-1060.
Ge, Y., MacDonald, D. L., Holroyd, K. J., Thornsberry, C., Wexler, H., &; Zasloff, M. (1999). In vitro Antibacterial Properties of Pexiganan, an Analog of Magainin. Antimicrob Agents Chemother, 43(4), 782-788.
Gear, M. W. L., Truelove, S. C., &; Whitehead, R. (1971). Gastric ulcer and gastritis. Gut, 12(8), 639-645.
George B. Stefano, G. L. F., Yannick Goumon, Tobias Esch. (2005). Pain, immunity, opiate and opioid compounds and health. Med Sci Monit, 11(5), MS47-53.
Gerhard, M., Lehn, N., Neumayer, N., Boren, T., Rad, R., Schepp, W.,Prinz, C. (1999). Clinical relevance of the Helicobacter pylori gene for blood-group antigen-binding adhesin. Proc Natl Acad Sci U S A, 96(22), 12778-12783.
Giacometti, A., Cirioni, O., Del Prete, M. S., Barchiesi, F., &; Scalise, G. (2000). Short-Term Exposure to Membrane-Active Antibiotics Inhibits Cryptosporidium parvum Infection in Cell Culture. Antimicrob Agents Chemother, 44(12), 3473-3475.
Giacometti, A., Cirioni, O., Ghiselli, R., Orlando, F., Kamysz, W., Rocchi, M., Scalise, G. (2005). Effects of pexiganan alone and combined with betalactams in experimental endotoxic shock. Peptides, 26(2), 207-216.
Giacometti, A., Cirioni, O., Greganti, G., Quarta, M., &; Scalise, G. (1998). In vitro Activities of Membrane-Active Peptides against Gram-Positive and Gram-Negative Aerobic Bacteria. Antimicrob Agents Chemother, 42(12), 3320-3324.
Goll, R., Gruber, F., Olsen, T., Cui, G., Raschpichler, G., Buset, M., Florholmen, J. (2007). Helicobacter pylori stimulates a mixed adaptive immune response with a strong T-regulatory component in human gastric mucosa. Helicobacter, 12(3), 185-192.
Goodman, K. J., Joyce, S. L., &; Ismond, K. P. (2006). Extragastric diseases associated with Helicobacter pylori infection. Curr Gastroenterol Rep, 8(6), 458-464.
Goodwin, C. S., Armstrong, J. A., Chilvers, T., Peters, M., Collins, M. D., Sly, L., Harper, W. E. S. (1989). Transfer of Campylobacter pylori and Campylobacter mustelae to Helicobacter gen. nov. as Helicobacter pylori comb. nov. and Helicobacter mustelae comb. nov., Respectively. International Journal of Systematic Bacteriology, 39(4), 397-405.
Goodwin, C. S., McCulloch, R. K., Armstrong, J. A., &; Wee, S. H. (1985). Unusual cellular fatty acids and distinctive ultrastructure in a new spiral bacterium (Campylobacter pyloridis) from the human gastric mucosa. J Med Microbiol, 19(2), 257-267.
Gordon, Y. J., Romanowski, E. G., &; McDermott, A. M. (2005). A Review of Antimicrobial Peptides and Their Therapeutic Potential as Anti-Infective Drugs. Current eye research, 30(7), 505-515.
Gottler, L. M., &; Ramamoorthy, A. (2009). Structure, membrane orientation, mechanism, and function of pexiganan — A highly potent antimicrobial peptide designed from magainin. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1788(8), 1680-1686.
Goumon, Y., Lugardon, K., Kieffer, B., Lefèvre, J.-F., Van Dorsselaer, A., Aunis, D., &; Metz-Boutigue, M.-H. (1998). Characterization of Antibacterial COOH-terminal Proenkephalin-A-derived Peptides (PEAP) in Infectious Fluids: Importance Of Enkelytin, The Antibacterial Peap209–237 Secreted By Stimulated Chromaffin Cells. Journal of Biological Chemistry, 273(45), 29847-29856.
Graham, D. Y., Malaty, H. M., Evans, D. G., Evans, D. J., Jr., Klein, P. D., &; Adam, E. (1991). Epidemiology of Helicobacter pylori in an asymptomatic population in the United States. Effect of age, race, and socioeconomic status. Gastroenterology, 100(6), 1495-1501.
Gray, B. M., Fontaine, C. A., Poe, S. A., &; Eaton, K. A. (2013). Complex T Cell Interactions Contribute to Helicobacter pylori Gastritis in Mice. Infection and Immunity, 81(3), 740-752.
Guani-Guerra, E., Santos-Mendoza, T., Lugo-Reyes, S. O., &; Teran, L. M. (2010). Antimicrobial peptides: general overview and clinical implications in human health and disease. [Review]. Clinical Immunology, 135(1), 1-11.
Guntupalli, K., Dean, N., Morris, P. E., Bandi, V., Margolis, B., Rivers, E., Dellinger, R. P. (2013). A phase 2 randomized, double-blind, placebo-controlled study of the safety and efficacy of talactoferrin in patients with severe sepsis. Crit Care Med, 41(3), 706-716.

Gupta, V. R., Patel, H. K., Kostolansky, S. S., Ballivian, R. A., Eichberg, J., &; Blanke, S. R. (2008). Sphingomyelin Functions as a Novel Receptor for Helicobacter pylori VacA. PLoS Pathog, 4(5), e1000073.
Gwack, J., Shin, A., Kim, C. S., Ko, K. P., Kim, Y., Jun, J. K., Yoo, K. Y. (2006). CagA-producing Helicobacter pylori and increased risk of gastric cancer: a nested case-control study in Korea. Br J Cancer, 95(5), 639-641.
Gwadz, R. W., Kaslow, D., Lee, J. Y., Maloy, W. L., Zasloff, M., &; Miller, L. H. (1989). Effects of magainins and cecropins on the sporogonic development of malaria parasites in mosquitoes. Infection and Immunity, 57(9), 2628-2633.
Ha, N. C., Oh, S. T., Sung, J. Y., Cha, K. A., Lee, M. H., &; Oh, B. H. (2001). Supramolecular assembly and acid resistance of Helicobacter pylori urease. Nat Struct Biol, 8(6), 505-509.
Hancock, R. E. W., &; Sahl, H.-G. (2006). Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotech, 24(12), 1551-1557.
Hancock, R. E., &; Diamond, G. (2000). The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol, 8(9), 402-410.
Hancock, R. E., &; Scott, M. G. (2000). The role of antimicrobial peptides in animal defenses. Proceedings of the National Academy of Sciences of the United States of America, 97(16), 8856-8861.
Hansson, L. E., Engstrand, L., Nyren, O., Evans, D. J., Jr., Lindgren, A., Bergstrom, R., Tracz, P. (1993). Helicobacter pylori infection: independent risk indicator of gastric adenocarcinoma. Gastroenterology, 105(4), 1098-1103.
Harrington, J. M. (2011). Antimicrobial peptide killing of African trypanosomes. Parasite Immunology, 33(8), 461-469.
Harris, R. A., Owens, D. K., Witherell, H., &; Parsonnet, J. (1999). Helicobacter pylori and Gastric Cancer: What Are the Benefits of Screening Only for the CagA Phenotype of H. pylori? Helicobacter, 4(2), 69-76.
Harris, S. M., Zhang, L., Parente, J., Rodeheaver, G. T., &; Falla, T. J. (2004). 111 HB-50: A Pre-Clinical Study of a Prophylactic for Wound Infection. Wound Repair and Regeneration, 12(2), A29-A29.
Hashim, H., Azmin, S., Razlan, H., Yahya, N. W., Tan, H. J., Manaf, M. R. A., &; Ibrahim, N. M. (2014). Eradication of Helicobacter pylori Infection Improves Levodopa Action, Clinical Symptoms and Quality of Life in Patients with Parkinson''s Disease. PLoS One, 9(11), e112330.
Hatakeyama, M. (2006). The role of Helicobacter pylori CagA in gastric carcinogenesis. Int J Hematol, 84(4), 301-308.
Hatakeyama, M. Helicobacter pylori CagA and Gastric Cancer: A Paradigm for Hit-and-Run Carcinogenesis. Cell Host &; Microbe, 15(3), 306-316.
Hatakeyama, M., &; Higashi, H. (2005). Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis. Cancer Science, 96(12), 835-843.
Heine, H., Muller-Loennies, S., Brade, L., Lindner, B., &; Brade, H. (2003). Endotoxic activity and chemical structure of lipopolysaccharides from Chlamydia trachomatis serotypes E and L2 and Chlamydophila psittaci 6BC. Eur J Biochem, 270(3), 440-450.
Herce, H. D., Garcia, A. E., Litt, J., Kane, R. S., Martin, P., Enrique, N., Milesi, V. (2009). Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides. Biophysical Journal, 97(7), 1917-1925.
Hilpert, K., Volkmer-Engert, R., Walter, T., &; Hancock, R. E. W. (2005). High-throughput generation of small antibacterial peptides with improved activity. Nat Biotech, 23(8), 1008-1012.
Hino, B., Eliakim, R., Levine, A., Sprecher, H., Berkowitz, D., Hartman, C., Shamir, R. (2004). Comparison of invasive and non-invasive tests diagnosis and monitoring of Helicobacter pylori infection in children. J Pediatr Gastroenterol Nutr, 39(5), 519-523.
Hipfel, R., Schittek, B., Bodingbauer, Y., &; Garbe, C. (2000). Specifically regulated genes in malignant melanoma tissues identified by subtractive hybridization. Br J Cancer, 82(6), 1149-1157.
Hsieh, J.-C., Pan, C.-Y., &; Chen, J.-Y. (2010). Tilapia hepcidin (TH)2-3 as a transgene in transgenic fish enhances resistance to Vibrio vulnificus infection and causes variations in immune-related genes after infection by different bacterial species. Fish Shellfish Immunol, 29(3), 430-439.
Huang, H. N., Pan, C. Y., Chan, Y. L., Chen, J. Y., &; Wu, C. J. (2014). Use of the antimicrobial peptide pardaxin (GE33) to protect against methicillin-resistant Staphylococcus aureus infection in mice with skin injuries. Antimicrob Agents Chemother, 58(3), 1538-1545.
Huang, H. N., Pan, C. Y., Rajanbabu, V., Chan, Y. L., Wu, C. J., &; Chen, J. Y. (2011). Modulation of immune responses by the antimicrobial peptide, epinecidin (Epi)-1, and establishment of an Epi-1-based inactivated vaccine. Biomaterials, 32(14), 3627-3636.
Huang, H. N., Rajanbabu, V., Pan, C. Y., Chan, Y. L., Wu, C. J., &; Chen, J. Y. (2013). Use of the antimicrobial peptide Epinecidin-1 to protect against MRSA infection in mice with skin injuries. Biomaterials, 34(38), 10319-10327.
Huang, H.-N., Pan, C.-Y., Chan, Y.-L., Chen, J.-Y., &; Wu, C.-J. (2014). Use of the Antimicrobial Peptide Pardaxin (GE33) To Protect against Methicillin-Resistant Staphylococcus aureus Infection in Mice with Skin Injuries. Antimicrobial Agents and Chemotherapy, 58(3), 1538-1545.
Huang, H.-N., Pan, C.-Y., Rajanbabu, V., Chan, Y.-L., Wu, C.-J., &; Chen, J.-Y. (2011). Modulation of immune responses by the antimicrobial peptide, epinecidin (Epi)-1, and establishment of an Epi-1-based inactivated vaccine. Biomaterials, 32(14), 3627-3636.
Huang, H.-N., Rajanbabu, V., Pan, C.-Y., Chan, Y.-L., Wu, C.-J., &; Chen, J.-Y. (2013). Use of the antimicrobial peptide Epinecidin-1 to protect against MRSA infection in mice with skin injuries. Biomaterials, 34(38), 10319-10327.
Huang, P.-H., Chen, J.-Y., &; Kuo, C.-M. (2007). Three different hepcidins from tilapia, Oreochromis mossambicus: Analysis of their expressions and biological functions. Molecular Immunology, 44(8), 1922-1934.
Huang, T. C., &; Chen, J. Y. (2013). Proteomic and functional analysis of zebrafish after administration of antimicrobial peptide epinecidin-1. Fish Shellfish Immunol, 34(2), 593-598.
Huang, Y., Huang, J., &; Chen, Y. (2010). Alpha-helical cationic antimicrobial peptides: relationships of structure and function. Protein Cell, 1(2), 143-152.
Hurdle, J. G., O''Neill, A. J., Chopra, I., &; Lee, R. E. (2011). Targeting bacterial membrane function: an underexploited mechanism for treating persistent infections. Nat Rev Microbiol, 9(1), 62-75.
Hussein, N. R., Argent, R. H., Marx, C. K., Patel, S. R., Robinson, K., &; Atherton, J. C. (2010). Helicobacter pylori dupA Is Polymorphic, and Its Active Form Induces Proinflammatory Cytokine Secretion by Mononuclear Cells. Journal of Infectious Diseases, 202(2), 261-269.
Ilver, D., Arnqvist, A., Ogren, J., Frick, I. M., Kersulyte, D., Incecik, E. T., Boren, T. (1998). Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging. Science, 279(5349), 373-377.
Isaacs, C. E., Jia, J. H., &; Xu, W. (2004). A lipid-peptide microbicide inactivates herpes simplex virus. Antimicrob Agents Chemother, 48(8), 3182-3184.
Isaacson, T., Soto, A., Iwamuro, S., Knoop, F. C., &; Conlon, J. M. (2002). Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. Peptides, 23(3), 419-425.
Isaacson, T., Soto, A., Iwamuro, S., Knoop, F. C., &; Conlon, J. M. (2002). Antimicrobial peptides with atypical structural features from the skin of the Japanese brown frog Rana japonica. Peptides, 23(3), 419-425.
Islas-Rodrìguez, A. E., Marcellini, L., Orioni, B., Barra, D., Stella, L., &; Mangoni, M. L. (2009). Esculentin 1–21: a linear antimicrobial peptide from frog skin with inhibitory effect on bovine mastitis-causing bacteria. Journal of Peptide Science, 15(9), 607-614.
Iwamoto, H., Czajkowsky, D. M., Cover, T. L., Szabo, G., &; Shao, Z. (1999). VacA from Helicobacter pylori: a hexameric chloride channel. FEBS Lett, 450(1-2), 101-104.
Iwao, E., Yamamoto, K., Yokoyama, Y., Hirayama, F., &; Haga, K. (2004). Potent antibacterial activity of Y-754, a novel benzimidazole compound with selective action against Helicobacter pylori. J Infect Chemother, 10(2), 90-96.
James, G. (2010). Universal Bacterial Identification by PCR and DNA Sequencing of 16S rRNA Gene. 209-214.
Jayamani, E., Rajamuthiah, R., Larkins-Ford, J., Fuchs, B. B., Conery, A. L., Vilcinskas, A., Mylonakis, E. (2015). Insect-Derived Cecropins Display Activity against Acinetobacter baumannii in a Whole-Animal High-Throughput Caenorhabditis elegans Model. Antimicrob Agents Chemother, 59(3), 1728-1737.
Ji, H.-x., Zou, Y.-l., Duan, J.-j., Jia, Z.-r., Li, X.-j., Wang, Z., Yang, Y. (2013). The Synthetic Melanocortin CKPV2 Exerts Anti-Fungal and Anti-Inflammatory Effects against Candida albicans Vaginitis via Inducing Macrophage M2 Polarization. PLoS ONE, 8(2), e56004.
Jiang, Z., Vasil, A. I., Hale, J. D., Hancock, R. E. W., Vasil, M. L., &; Hodges, R. S. (2008b). Effects of Net Charge and the Number of Positively Charged Residues on the Biological Activity of Amphipathic α-Helical Cationic Antimicrobial Peptides. Biopolymers, 90(3), 369-383.
Jones, D. M., Curry, A., &; Fox, A. J. (1985). An Ultrastructural Study of the Gastric Campylobacter-like Organism ‘Campylobacter pyloridis''. Journal of General Microbiology, 131(9), 2335-2341.
Jones, J. C., Turpin, E. A., Bultmann, H., Brandt, C. R., &; Schultz-Cherry, S. (2006). Inhibition of Influenza Virus Infection by a Novel Antiviral Peptide That Targets Viral Attachment to Cells. Journal of Virology, 80(24), 11960-11967.
Jones, K. R., Cha, J. H., &; Merrell, D. S. (2008). Who''s Winning the War? Molecular Mechanisms of Antibiotic Resistance in Helicobacter pylori. Curr Drug ther, 3(3), 190-203.
K, B. (2004). Why it is important to continue antibacterial drug discovery. ASM News, 70(6), 282-287.
Kabir, S. (2011). The Role of Interleukin-17 in the Helicobacter pylori Induced Infection and Immunity. Helicobacter, 16(1), 1-8.
Kao, J. Y., Zhang, M., Miller, M. J., Mills, J. C., Wang, B., Liu, M., Luther, J. (2010). Helicobacter pylori immune escape is mediated by dendritic cell-induced Treg skewing and Th17 suppression in mice. Gastroenterology, 138(3), 1046-1054.
Karttunen, R., Karttunen, T., Ekre, H. P., &; MacDonald, T. T. (1995). Interferon gamma and interleukin 4 secreting cells in the gastric antrum in Helicobacter pylori positive and negative gastritis. Gut, 36(3), 341-345.
Kasai, K., &; Kobayashi, R. (1919). The Stomach Spirochete Occurring in Mammals. The Journal of Parasitology, 6(1), 1-10.
Kasper, G., &; Dickgiesser, N. (1984). Isolation of campylobacter-like bacteria from gastric epithelium. Infection, 12(3), 179-180.
Kasper, G., &; Dickgiesser, N. (1985). Isolation from gastric epithelium of Campylobacter-like bacteria that are distinct from "Campylobacter pyloridis” Lancet, 1(8420), 111-112.
Khademi, F., Faghri, J., Poursina, F., Esfahani, B. N., Moghim, S., Fazeli, H., Safaei, H. G. (2013). Resistance pattern of Helicobacter pylori strains to clarithromycin, metronidazole, and amoxicillin in Isfahan, Iran. J Res Med Sci, 18(12), 1056-1060.
Khara, J. S., Wang, Y., Ke, X.-Y., Liu, S., Newton, S. M., Langford, P. R., Ee, P. L. R. (2014). Anti-mycobacterial activities of synthetic cationic α-helical peptides and their synergism with rifampicin. Biomaterials, 35(6), 2032-2038.
Khedmat, H., Karami, A., Safiri, Z., Amini, M., Bakhtiari, A., Karbasi, A., Taheri, S. (2012). Helicobacter pylori genotypes can predict gastric tissue histopathology: A longitudinal study of Iranian patients. Journal of Infection and Public Health, 5(2), 153-158.
Khoshnood, A., Hakimi, P., Salman-Roghani, H., &; Reza Mirjalili, M. (2014). Replacement of clarithromycin with azithromycin in triple therapy regimens for the eradication of Helicobacter pylori: A randomized clinical trial. Journal of Medicine and Life, 7(2), 254-259.
King, L. E., &; Fraker, P. J. (1991). Flow cytometric analysis of the phenotypic distribution of splenic lymphocytes in zinc-deficient adult mice. J Nutr, 121(9), 1433-1438.
Klevens, R. M., Edwards, J. R., Richards, C. L., Jr., Horan, T. C., Gaynes, R. P., Pollock, D. A., &; Cardo, D. M. (2007). Estimating health care-associated infections and deaths in U.S. hospitals, 2002. Public Health Rep, 122(2), 160-166.
Kłodzińska, E., Szumski, M., Dziubakiewicz, E., Hrynkiewicz, K., Skwarek, E., Janusz, W., &; Buszewski, B. (2010). Effect of zeta potential value on bacterial behavior during electrophoretic separation. Electrophoresis, 31(9), 1590-1596.
Knipp, U., Birkholz, S., Kaup, W., &; Opferkuch, W. (1996). Partial characterization of a cell proliferation-inhibiting protein produced by Helicobacter pylori. Infect Immun, 64(9), 3491-3496.
Kolar, S., Luca, V., Baidouri, H., Mannino, G., McDermott, A., &; Mangoni, M. (2015). Esculentin-1a(1-21)NH2: a frog skin-derived peptide for microbial keratitis. Cellular and Molecular Life Sciences, 72(3), 617-627.
Koyama, T., Michael Conlon, J., &; Iwamuro, S. (2011). Molecular Cloning and Characterization of cDNAs Encoding Biosynthetic Precursors for the Antimicrobial Peptides Japonicin-1Ja, Japonicin-2Ja, and Temporin-1Ja in the Japanese Brown Frog, Rana japonica. Zoological Science, 28(5), 339-347.
Krishnakumari, V., Rangaraj, N., &; Nagaraj, R. (2009). Antifungal Activities of Human Beta-Defensins HBD-1 to HBD-3 and Their C-Terminal Analogs Phd1 to Phd3. Antimicrob Agents Chemother, 53(1), 256-260.
Kronsteiner, B., Bassaganya-Riera, J., Philipson, C., Viladomiu, M., Carbo, A., Pedragosa, M., Hontecillas, R. (2013). Helicobacter pylori Infection in a Pig Model Is Dominated by Th1 and Cytotoxic CD8(+) T Cell Responses. Infect Immun, 81(10), 3803-3813.
Kuipers, E. J. (1999). Review article: exploring the link between Helicobacter pylori and gastric cancer. Alimentary Pharmacology and Therapeutics, 13, 3-11.
Kusters, J. G., van Vliet, A. H. M., &; Kuipers, E. J. (2006). Pathogenesis of Helicobacter pylori Infection. Clinical Microbiology Reviews, 19(3), 449-490.
Laforce, F. M., &; Boose, D. S. (1981). Sublethal damage of Escherichia coli by lung lavage. The American review of respiratory disease, 124(6), 733-737.
Lai, Y., Villaruz, A. E., Li, M., Cha, D. J., Sturdevant, D. E., &; Otto, M. (2007). The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci. Mol Microbiol, 63(2), 497-506.
Lamb, H., &; Wiseman, L. (1998). Pexiganan Acetate. Drugs, 56(6), 1047-1052.
Lazic, S. (2008). Why we should use simpler models if the data allow this: relevance for ANOVA designs in experimental biology. BMC Physiology, 8(1), 16.
Lee, J.-K., Park, S.-C., Hahm, K.-S., &; Park, Y. (2014). A helix-PXXP-helix peptide with antibacterial activity without cytotoxicity against MDRPA-infected mice. Biomaterials, 35(3), 1025-1039.
Lee, P. H. A., Rudisill, J. A., Lin, K. H., Zhang, L., Harris, S. M., Falla, T. J., &; Gallo, R. L. (2004). HB-107, a nonbacteriostatic fragment of the antimicrobial peptide cecropin B, accelerates murine wound repair. Wound Repair and Regeneration, 12(3), 351-358.
Lee, S. A., Kim, Y. K., Lim, S. S., Zhu, W. L., Ko, H., Shin, S. Y., Kim, Y. (2007). Solution structure and cell selectivity of piscidin 1 and its analogues. Biochemistry, 46(12), 3653-3663.
Lee, S. C., Pan, C. Y., &; Chen, J. Y. (2012). The antimicrobial peptide, epinecidin-1, mediates secretion of cytokines in the immune response to bacterial infection in mice. Peptides, 36(1), 100-108.
Lee, Y.-C., Liou, J.-M., Wu, M.-S., Wu, C.-Y., &; Lin, J.-T. (2008). Eradication of Helicobacter pylori to Prevent Gastroduodenal Diseases: Hitting more than One Bird with the Same Stone. Therapeutic Advances in Gastroenterology, 1(2), 111-120.
Lee, Y.-C., Liou, J.-M., Wu, M.-S., Wu, C.-Y., &; Lin, J.-T. (2008). Eradication of Helicobacter pylori to Prevent Gastroduodenal Diseases: Hitting more than One Bird with the Same Stone. Therapeutic Advances in Gastroenterology, 1(2), 111-120.
Levings, M. K., Gregori, S., Tresoldi, E., Cazzaniga, S., Bonini, C., &; Roncarolo, M. G. (2005). Differentiation of Tr1 cells by immature dendritic cells requires IL-10 but not CD25+CD4+ Tr cells. Blood, 105(3), 1162-1169.
Li, C., Ha, T., Ferguson, D., Jr., Chi, D., Zhao, R., Patel, N., Thomas, E. (1996). A newly developed PCR assay ofH. pylori in gastric biopsy, saliva, and feces. Digestive Diseases and Sciences, 41(11), 2142-2149.
Li, H., Cheng, J. W., Yu, H. Y., Xin, Y., Tang, L., &; Ma, Y. (2013). Effect of the antimicrobial peptide D-Nal-Pac-525 on the growth of Streptococcus mutans and its biofilm formation. J Microbiol Biotechnol, 23(8), 1070-1075.
Li, P., Poon, Y. F., Li, W., Zhu, H. Y., Yeap, S. H., Cao, Y., Chan-Park, M. B. (2011). A polycationic antimicrobial and biocompatible hydrogel with microbe membrane suctioning ability. Nat Mater, 10(2), 149-156.
Liang, Y.-Y., Zhang, L.-M., Li, W., &; Chen, R.-F. (2007). Polysaccharide-modified iron oxide nanoparticles as an effective magnetic affinity adsorbent for bovine serum albumin. Colloid and Polymer Science, 285(11), 1193-1199.
Lin, S. B., Fan, T. W., Wu, J. L., Hui, C. F., &; Chen, J. Y. (2009). Immune response and inhibition of bacterial growth by electrotransfer of plasmid DNA containing the antimicrobial peptide, epinecidin-1, into zebrafish muscle. Fish Shellfish Immunol, 26(3), 451-458.
Lin, W. J., Chien, Y. L., Pan, C. Y., Lin, T. L., Chen, J. Y., Chiu, S. J., &; Hui, C. F. (2009). Epinecidin-1, an antimicrobial peptide from fish (Epinephelus coioides) which has an antitumor effect like lytic peptides in human fibrosarcoma cells. Peptides, 30(2), 283-290.
Lin, Y.-H., Tsai, S.-C., Lai, C.-H., Lee, C.-H., He, Z. S., &; Tseng, G.-C. (2013). Genipin-cross-linked fucose–chitosan/heparin nanoparticles for the eradication of Helicobacter pylori. Biomaterials, 34(18), 4466-4479.
Lindberg, I., &; White, L. (1986). Distribution of immunoreactive peptide B in the rat brain. Biochemical and Biophysical Research Communications, 139(3), 1024-1032.

Logan, R. H. (1994). CONFERENCE: Helicobacter pylori and gastric cancer. The Lancet, 344(8929), 1078-1079.

Loh, B., Grant, C., &; Hancock, R. E. (1984). Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa. Antimicrob Agents Chemother, 26(4), 546-551.
Lominadze, G., Powell, D. W., Luerman, G. C., Link, A. J., Ward, R. A., &; McLeish, K. R. (2005). Proteomic Analysis of Human Neutrophil Granules. Molecular &; Cellular Proteomics, 4(10), 1503-1521.
Lowrie, A. G., Wigmore, S. J., Wright, D. J., Waddell, I. D., &; Ross, J. A. (2006). Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues. Br J Cancer, 94(11), 1663-1671.
Luca, V., Stringaro, A., Colone, M., Pini, A., &; Mangoni, M. (2013). Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa. Cellular and Molecular Life Sciences, 70(15), 2773-2786.
Luengo, J., Weiss, B., Schneider, M., Ehlers, A., Stracke, F., Konig, K., Schaefer, U. F. (2006). Influence of nanoencapsulation on human skin transport of flufenamic acid. [Research Support, Non-U.S. Gov''t]. Skin Pharmacol Physiol, 19(4), 190-197.
Lundgren, A., Strömberg, E., Sjöling, Å., Lindholm, C., Enarsson, K., Edebo, A.,Lundin, B. S. (2005). Mucosal FOXP3-Expressing CD4+ CD25high Regulatory T Cells in Helicobacter pylori-Infected Patients. Infect Immun, 73(1), 523-531.
Luzza, F., Parrello, T., Monteleone, G., Sebkova, L., Romano, M., Zarrilli, R., Pallone, F. (2000). Up-Regulation of IL-17 Is Associated with Bioactive IL-8 Expression in Helicobacter pylori-Infected Human Gastric Mucosa. The Journal of Immunology, 165(9), 5332-5337.
Lv, Y., Wang, J., Gao, H., Wang, Z., Dong, N., Ma, Q., &; Shan, A. (2014). Antimicrobial Properties and Membrane-Active Mechanism of a Potential α-Helical Antimicrobial Derived from Cathelicidin PMAP-36. PLoS One, 9(1), e86364.
Maekawa, T., Kinoshita, Y., Matsushima, Y., Okada, A., Fukui, H., Waki, S., Chiba, T. (1997). Helicobacter pylori induces proinflammatory cytokines and major histocompatibility complex class II antigen in mouse gastric epithelial cells. Journal of Laboratory and Clinical Medicine, 130(4), 442-449.
Mahdavi, J., Sonden, B., Hurtig, M., Olfat, F. O., Forsberg, L., Roche, N., Boren, T. (2002). Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation.
Mai, U. E., Perez-Perez, G. I., Wahl, L. M., Wahl, S. M., Blaser, M. J., &; Smith, P. D. (1991a). Soluble surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism. Journal of Clinical Investigation, 87(3), 894-900.
Mai, U. E., Perez-Perez, G. I., Wahl, L. M., Wahl, S. M., Blaser, M. J., &; Smith, P. D. (1991b). Soluble surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism. J Clin Invest, 87(3), 894-900.
Makobongo, M. O., Gancz, H., Carpenter, B. M., McDaniel, D. P., &; Merrell, D. S. (2012). The oligo-acyl lysyl antimicrobial peptide C(1)(2)K-2beta(1)(2) exhibits a dual mechanism of action and demonstrates strong in vivo efficacy against Helicobacter pylori. Antimicrob Agents Chemother, 56(1), 378-390.
Makobongo, M. O., Gancz, H., Carpenter, B. M., McDaniel, D. P., &; Merrell, D. S. (2012). The oligo-acyl lysyl antimicrobial peptide C(1)(2)K-2beta(1)(2) exhibits a dual mechanism of action and demonstrates strong in vivo efficacy against Helicobacter pylori. Antimicrob Agents Chemother, 56(1), 378-390.
Makobongo, M. O., Kovachi, T., Gancz, H., Mor, A., &; Merrell, D. S. (2009). In vitro antibacterial activity of acyl-lysyl oligomers against Helicobacter pylori. Antimicrobial Agents and Chemotherapy, 53(10), 4231-4239.
Malfertheiner, P., Megraud, F., O’Morain, C., Bazzoli, F., El-Omar, E., Graham, D., Kuipers, E. J. (2007). Current concepts in the management of Helicobacter pylori infection: the Maastricht III Consensus Report. Gut, 56(6), 772-781.
Malkoski, M., Dashper, S. G., O''Brien-Simpson, N. M., Talbo, G. H., Macris, M., Cross, K. J., &; Reynolds, E. C. (2001). Kappacin, a Novel Antibacterial Peptide from Bovine Milk. Antimicrob Agents Chemother, 45(8), 2309-2315.
Malmsten, M. (2011). Antimicrobial and antiviral hydrogels. Soft Matter, 7(19), 8725-8736.
Mangoni, M. L. (2006). Temporins, anti-infective peptides with expanding properties. Cellular and Molecular Life Sciences CMLS, 63(9), 1060-1069.
Mangoni, M. L., Papo, N., Mignogna, G., Andreu, D., Shai, Y., Barra, D., &; Simmaco, M. (2003). Ranacyclins, a New Family of Short Cyclic Antimicrobial Peptides:  Biological Function, Mode of Action, and Parameters Involved in Target Specificity Biochemistry, 42(47), 14023-14035.
Mangoni, M. L., Saugar, J. M., Dellisanti, M., Barra, D., Simmaco, M., &; Rivas, L. (2005). Temporins, Small Antimicrobial Peptides with Leishmanicidal Activity. Journal of Biological Chemistry, 280(2), 984-990.
Manzo, G., Sanna, R., Casu, M., Mignogna, G., Mangoni, M. L., Rinaldi, A. C., &; Scorciapino, M. A. (2012). Toward an improved structural model of the frog-skin antimicrobial peptide esculentin-1b(1-18). Biopolymers, 97(11), 873-881.
Marchetti, M., Arico, B., Burroni, D., Figura, N., Rappuoli, R., &; Ghiara, P. (1995). Development of a mouse model of Helicobacter pylori infection that mimics human disease. Science, 267(5204), 1655-1658.
Marcos, N. T., Magalhaes, A., Ferreira, B., Oliveira, M. J., Carvalho, A. S., Mendes, N., Reis, C. A. (2008). Helicobacter pylori induces beta3GnT5 in human gastric cell lines, modulating expression of the SabA ligand sialyl-Lewis x. J Clin Invest, 118(6), 2325-2336.
Marin, A. C., McNicholl, A. G., &; Gisbert, J. P. (2013). A review of rescue regimens after clarithromycin-containing triple therapy failure (for Helicobacter pylori eradication). Expert Opin Pharmacother, 14(7), 843-861.
Marr, A. K., Gooderham, W. J., &; Hancock, R. E. W. (2006). Antibacterial peptides for therapeutic use: obstacles and realistic outlook. Current Opinion in Pharmacology, 6(5), 468-472.
Marshall, B. J., &; Warren, J. R. (1984). Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration. Lancet, 1(8390), 1311-1315.
Marshall, B. J., McGechie, D. B., Rogers, P. A., &; Glancy, R. J. (1985). Pyloric Campylobacter infection and gastroduodenal disease. Med J Aust, 142(8), 439-444.
Marshall, N. B., Oda, S. K., London, C. A., Moulton, H. M., Iversen, P. L., Kerkvliet, N. I., &; Mourich, D. V. (2007). Arginine-rich cell-penetrating peptides facilitate delivery of antisense oligomers into murine leukocytes and alter pre-mRNA splicing. J Immunol Methods, 325(1-2), 114-126.
Matsuyama, N., Kirikae, T., Kirikae, F., Hashimoto, M., Amanot, K., Hayashi, S., Nakano, M. (2001). Non-standard biological activities of lipopolysaccharide from Helicobacter pylori. J Med Microbiol, 50(10), 865-869.
McClanahan, J. R., Peyyala, R., Mahajan, R., Montelaro, R. C., Novak, K. F., &; Puleo, D. A. (2011). Bioactivity of WLBU2 peptide antibiotic in combination with bioerodible polymer. International Journal of Antimicrobial Agents, 38(6), 530-533.
McColl, K. E. L. (2010). Helicobacter pylori Infection. New England Journal of Medicine, 362(17), 1597-1604.
McDaniel, D. P., &; Roberson, R. W. (2000). Microtubules Are required for motility and positioning of vesicles and mitochondria in hyphal tip cells of Allomyces macrogynus. Fungal Genetics and Biology, 31(3), 233-244.
McDaniel, D. P., &; Roberson, R. W. (2000). Microtubules Are required for motility and positioning of vesicles and mitochondria in hyphal tip cells of Allomyces macrogynus. Fungal Genet Biol, 31(3), 233-244.
McDaniel, D. P., &; Roberson, R. W. (2000a). Microtubules Are required for motility and positioning of vesicles and mitochondria in hyphal tip cells of Allomyces macrogynus. Fungal Genetics and Biology, 31(3), 233-244.
McDaniel, D. P., &; Roberson, R. W. (2000b). Microtubules Are required for motility and positioning of vesicles and mitochondria in hyphal tip cells of Allomyces macrogynus. Fungal Genet Biol, 31(3), 233-244.
McGee, D. J., George, A. E., Trainor, E. A., Horton, K. E., Hildebrandt, E., &; Testerman, T. L. (2011). Cholesterol Enhances Helicobacter pylori Resistance to Antibiotics and LL-37. Antimicrobial Agents and Chemotherapy, 55(6), 2897-2904.
Megraud, F. (2004). H pylori antibiotic resistance: prevalence, importance, and advances in testing. Gut, 53(9), 1374-1384.
Megraud, F., Coenen, S., Versporten, A., Kist, M., Lopez-Brea, M., Hirschl, A. M. Glupczynski, Y. (2013). Helicobacter pylori resistance to antibiotics in Europe and its relationship to antibiotic consumption., Gut, 62(1), 34-42.
Merodio, M., Arnedo, A., Renedo, M. J., &; Irache, J. M. (2001). Ganciclovir-loaded albumin nanoparticles: characterization and in vitro release properties. [Research Support, Non-U.S. Gov''t]. Eur J Pharm Sci, 12(3), 251-259.
Metz-Boutigue, M. H., Goumon, Y., Lugardon, K., Strub, J. M., &; Aunis, D. (1998). Antibacterial peptides are present in chromaffin cell secretory granules. Cell Mol Neurobiol, 18(2), 249-266.
Miehlke, S., Kirsch, C., Agha-Amiri, K., Günther, T., Lehn, N., Malfertheiner, P., Bayerdörffer, E. (2000). The Helicobacter pylori vacA s1, m1 genotype and cagA is associated with gastric carcinoma in Germany. International Journal of Cancer, 87(3), 322-327.
Mini, R., Annibale, B., Lahner, E., Bernardini, G., Figura, N., &; Santucci, A. (2006). Western blotting of total lysate of Helicobacter pylori in cases of atrophic body gastritis. Clin Chem, 52(2), 220-226.
Mirzaei, N., Poursina, F., Moghim, S., Rahimi, E., &; Safaei, H. G. (2014). The mutation of the rdxA gene in metronidazole-resistant Helicobacter pylori clinical isolates. Advanced Biomedical Research, 3, 90.
Mitchell, P., Germain, C., Fiori, P. L., Khamri, W., Foster, G. R., Ghosh, S., Lombardi, G. (2007). Chronic exposure to Helicobacter pylori impairs dendritic cell function and inhibits Th1 development. Infect Immun, 75(2), 810-819.
Mobley, H. L., Island, M. D., &; Hausinger, R. P. (1995). Molecular biology of microbial ureases. Microbiological Reviews, 59(3), 451-480.
Moerman, L., Bosteels, S., Noppe, W., Willems, J., Clynen, E., Schoofs, L., Verdonck, F. (2002). Antibacterial and antifungal properties of α-helical, cationic peptides in the venom of scorpions from southern Africa. European Journal of Biochemistry, 269(19), 4799-4810.
Montecucco, C., &; Rappuoli, R. (2001). Living dangerously: how Helicobacter pylori survives in the human stomach. Nat Rev Mol Cell Biol, 2(6), 457-466.
Moran, A. (1998). The products of Helicobacter pylori that induce inflammation. Eur J Gastroenterol Hepatol, 10(1).
Moran, A. P. (1995). Cell surface characteristics of Helicobacter pylori. FEMS Immunol Med Microbiol, 10(3-4), 271-280.
Moran, A. P. (2008). Relevance of fucosylation and Lewis antigen expression in the bacterial gastroduodenal pathogen Helicobacter pylori. Carbohydrate Research, 343(12), 1952-1965.
Morvan, A., Bachere, E., Da Silva, P. P., Pimenta, P., &; Mialhe, E. (1994). In vitro activity of the antimicrobial peptide magainin 1 against Bonamia ostreae, the intrahemocytic parasite of the flat oyster Ostrea edulis. Mol Mar Biol Biotechnol, 3(6), 327-333.
Müller, M., dela Peña, A., &; Derendorf, H. (2004). Issues in Pharmacokinetics and Pharmacodynamics of Anti-Infective Agents: Distribution in Tissue. Antimicrobial Agents and Chemotherapy, 48(5), 1441-1453.
Muotiala, A., Helander, I. M., Pyhala, L., Kosunen, T. U., &; Moran, A. P. (1992). Low biological activity of Helicobacter pylori lipopolysaccharide. Infect Immun, 60(4), 1714-1716.
Nagarwal, R. C., Kant, S., Singh, P. N., Maiti, P., &; Pandit, J. K. (2009). Polymeric nanoparticulate system: a potential approach for ocular drug delivery. J Control Release, 136(1), 2-13.
Nagy, T. A., Frey, M. R., Yan, F., Israel, D. A., Polk, D. B., &; Peek, R. M., Jr. (2009). Helicobacter pylori regulates cellular migration and apoptosis by activation of phosphatidylinositol 3-kinase signaling. J Infect Dis, 199(5), 641-651.
Ng, V. W., Chan, J. M., Sardon, H., Ono, R. J., Garcia, J. M., Yang, Y. Y., &; Hedrick, J. L. (2014). Antimicrobial hydrogels: a new weapon in the arsenal against multidrug-resistant infections. Adv Drug Deliv Rev, 78, 46-62.
Nielsen, H., Birkholz, S., Andersen, L. P., &; Moran, A. P. (1994). Neutrophil activation by Helicobacter pylori lipopolysaccharides. J Infect Dis, 170(1), 135-139.
NIH Consensus Conference. Helicobacter pylori in peptic ulcer disease. NIH Consensus Development Panel on Helicobacter pylori in Peptic Ulcer Disease. (1994). JAMA, 272(1), 65-69.
Nikaido, H. (2009). Multidrug Resistance in Bacteria. Annual review of biochemistry, 78, 119-146.
Nilsson, C., Skoglund, A., Moran, A. P., Annuk, H., Engstrand, L., &; Normark, S. (2006). An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection. Proc Natl Acad Sci U S A, 103(8), 2863-2868.
Nilsson, H. O., Pietroiusti, A., Gabrielli, M., Zocco, M. A., Gasbarrini, G., &; Gasbarrini, A. (2005). Helicobacter pylori and extragastric diseases--other Helicobacters. Helicobacter, 10 Suppl 1, 54-65
Nishizawa, T., Suzuki, H., Suzuki, M., Takahashi, M., &; Hibi, T. (2012). Proton pump inhibitor-amoxicillin-clarithromycin versus proton pump inhibitor-amoxicillin-metronidazole as first-line Helicobacter pylorieradication therapy. Journal of Clinical Biochemistry and Nutrition, 51(2), 114-116
Niyonsaba, F., Suzuki, A., Ushio, H., Nagaoka, I., Ogawa, H., &; Okumura, K. (2009). The human antimicrobial peptide dermcidin activates normal human keratinocytes. British Journal of Dermatology, 160(2), 243-249.
Nizet, V. (2006). Antimicrobial peptide resistance mechanisms of human bacterial pathogens. Curr Issues Mol Biol, 8(1), 11-26.
Noach, L. A., Bosma, N. B., Jansen, J., Hoek, F. J., van Deventer, S. J., &; Tytgat, G. N. (1994). Mucosal tumor necrosis factor-alpha, interleukin-1 beta, and interleukin-8 production in patients with Helicobacter pylori infection. Scand J Gastroenterol, 29(5), 425-429.
Noga, E. J., Silphaduang, U., Park, N. G., Seo, J. K., Stephenson, J., &; Kozlowicz, S. (2009). Piscidin 4, a novel member of the piscidin family of antimicrobial peptides. Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology, 152(4), 299-305.
Noga, E. J., Silphaduang, U., Park, N. G., Seo, J. K., Stephenson, J., &; Kozlowicz, S. (2009). Piscidin 4, a novel member of the piscidin family of antimicrobial peptides. Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology, 152(4), 299-305.
Nomura, A., Stemmermann, G. N., Chyou, P. H., Perez-Perez, G. I., &; Blaser, M. J. (1994). Helicobacter pylori infection and the risk for duodenal and gastric ulceration. Annals of Internal Medicine, 120(12), 977-981.
Nomura, A., Stemmermann, G. N., Chyou, P.-H., Kato, I., Perez-Perez, G. I., &; Blaser, M. J. (1991). Helicobacter pylori Infection and Gastric Carcinoma among Japanese Americans in Hawaii. New England Journal of Medicine, 325(16), 1132-1136.
Obonyo, M., Guiney, D. G., Harwood, J., Fierer, J., &; Cole, S. P. (2002). Role of Gamma Interferon in Helicobacter pylori Induction of Inflammatory Mediators during Murine Infection. Infection and Immunity, 70(6), 3295-3299.
Obonyo, M., Sabet, M., Cole, S. P., Ebmeyer, J., Uematsu, S., Akira, S., &; Guiney, D. G. (2007). Deficiencies of myeloid differentiation factor 88, Toll-like receptor 2 (TLR2), or TLR4 produce specific defects in macrophage cytokine secretion induced by Helicobacter pylori. Infect Immun, 75(5), 2408-2414.
Obonyo, M., Sabet, M., Cole, S. P., Ebmeyer, J., Uematsu, S., Akira, S., &; Guiney, D. G. (2007). Deficiencies of myeloid differentiation factor 88, Toll-like receptor 2 (TLR2), or TLR4 produce specific defects in macrophage cytokine secretion induced by Helicobacter pylori. Infect Immun, 75(5), 2408-2414.
OECD. Test No. 405: Acute eye irritation/corrosion: OECD Publishing.
OECD. Test No. 406: Skin Sensitisation: OECD Publishing.
OECD. Test No. 407: Repeated Dose 28-day Oral Toxicity Study in Rodents: OECD Publishing.
OECD. Test No. 423: Acute Oral toxicity - Acute Toxic Class Method: OECD Publishing.
Ogawa, T., Asai, Y., Sakai, Y., Oikawa, M., Fukase, K., Suda, Y., Tamura, T. (2003). Endotoxic and immunobiological activities of a chemically synthesized lipid A of Helicobacter pylori strain 206-1. FEMS Immunol Med Microbiol, 36(1-2), 1-7.
Ogawa, T., Asai, Y., Yamamoto, H., Taiji, Y., Jinno, T., Kodama, T., Ochiai, K. (2000). Immunobiological activities of a chemically synthesized lipid A of Porphyromonas gingivalis. FEMS Immunol Med Microbiol, 28(4), 273-281.
Ortíz-López, F. J., Monteiro, M. C., González-Menéndez, V., Tormo, J. R., Genilloud, O., Bills, G. F.,Reyes, F. (2015). Cyclic Colisporifungin and Linear Cavinafungins, Antifungal Lipopeptides Isolated from Colispora cavincola. Journal of Natural Products.
Pai, R., Wyle, F. A., Cover, T. L., Itani, R. M., Domek, M. J., &; Tarnawski, A. S. (1998). Helicobacter pylori culture supernatant interferes with epidermal growth factor-activated signal transduction in human gastric KATO III cells. Am J Pathol, 152(6), 1617-1624.
Palframan, S. L., Kwok, T., &; Gabriel, K. (2012). Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis. Frontiers in Cellular and Infection Microbiology, 2, 92.
Pan, C. Y., Chen, J. Y., Cheng, Y. S., Chen, C. Y., Ni, I. H., Sheen, J. F., Kuo, C. M. (2007). Gene expression and localization of the epinecidin-1 antimicrobial peptide in the grouper (Epinephelus coioides), and its role in protecting fish against pathogenic infection. DNA and Cell Biology, 26(6), 403-413.
Pan, C. Y., Chen, J. Y., Lin, T. L., &; Lin, C. H. (2009). In vitro activities of three synthetic peptides derived from epinecidin-1 and an anti-lipopolysaccharide factor against Propionibacterium acnes, Candida albicans, and Trichomonas vaginalis. Peptides, 30(6), 1058-1068.
Pan, C. Y., Wu, J. L., Hui, C. F., Lin, C. H., &; Chen, J. Y. (2011). Insights into the antibacterial and immunomodulatory functions of the antimicrobial peptide, epinecidin-1, against Vibrio vulnificus infection in zebrafish. Fish Shellfish Immunol, 31(6), 1019-1025.
Pan, C.-Y., Chen, J.-C., Chen, T.-L., Wu, J.-L., Hui, C.-F., &; Chen, J.-Y. (2015). Piscidin is Highly Active against Carbapenem-Resistant Acinetobacter baumannii and NDM-1-Producing Klebsiella pneumonia in a Systemic Septicaemia Infection Mouse Model. Mar Drugs, 13(4), 2287-2305.
Pan, C.-Y., Chen, J.-C., Sheen, J.-F., Lin, T.-L., &; Chen, J.-Y. (2014). Epinecidin-1 Has Immunomodulatory Effects, Facilitating Its Therapeutic Use in a Mouse Model of Pseudomonas aeruginosa Sepsis. Antimicrob Agents Chemother, 58(8), 4264-4274.
Pan, C.-Y., Chen, J.-Y., Cheng, Y.-S. E., Chen, C.-Y., Ni, I. H., Sheen, J.-F., Kuo, C.-M. (2007). Gene Expression and Localization of the Epinecidin-1 Antimicrobial Peptide in the Grouper (Epinephelus coioides), and Its Role in Protecting Fish Against Pathogenic Infection. DNA and Cell Biology, 26(6), 403-413.
Pan, C.-Y., Chen, J.-Y., Lin, T.-L., &; Lin, C.-H. (2009). In vitro activities of three synthetic peptides derived from epinecidin-1 and an anti-lipopolysaccharide factor against Propionibacterium acnes, Candida albicans, and Trichomonas vaginalis. Peptides, 30(6), 1058-1068.
Pan, C.-Y., Rajanbabu, V., Chen, J.-Y., Her, G. M., &; Nan, F.-H. (2010). Evaluation of the epinecidin-1 peptide as an active ingredient in cleaning solutions against pathogens. Peptides, 31(8), 1449-1458.
Papini, E., Satin, B., Norais, N., de Bernard, M., Telford, J. L., Rappuoli, R., &; Montecucco, C. (1998). Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin. Journal of Clinical Investigation, 102(4), 813-820.
Parkin, D. M. (2004). International variation. Oncogene, 23(38), 6329-6340.
Parsonnet, J., Friedman, G. D., Vandersteen, D. P., Chang, Y., Vogelman, J. H., Orentreich, N., &; Sibley, R. K. (1991). Helicobacter pylori Infection and the Risk of Gastric Carcinoma. New England Journal of Medicine, 325(16), 1127-1131.
Parsonnet, J., Hansen, S., Rodriguez, L., Gelb, A. B., Warnke, R. A., Jellum, E., Friedman, G. D. (1994). Helicobacter pylori Infection and Gastric Lymphoma. New England Journal of Medicine, 330(18), 1267-1271.
Parsonnet, J., Vandersteen, D., Goates, J., Sibley, R. K., Pritikin, J., &; Chang, Y. (1991). Helicobacter pylori Infection in Intestinal- and Diffuse-Type Gastric Adenocarcinomas. Journal of the National Cancer Institute, 83(9), 640-643.
Patel, A. R., Kulkarni, S., Nandekar, T. D., &; Vavia, P. R. (2008). Evaluation of alkyl polyglucoside as an alternative surfactant in the preparation of peptide-loaded nanoparticles. Journal of Microencapsulation, 25(8), 531-540.
Patel, J. D., O''Carra, R., Jones, J., Woodward, J. G., &; Mumper, R. J. (2007). Preparation and characterization of nickel nanoparticles for binding to his-tag proteins and antigens. Pharm Res, 24(2), 343-352.
Paulmann, M., Arnold, T., Linke, D., Ozdirekcan, S., Kopp, A., Gutsmann, T., Schittek, B. (2012). Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. J Biol Chem, 287(11), 8434-8443.
Peng, K. C., Lee, S. H., Hour, A. L., Pan, C. Y., Lee, L. H., &; Chen, J. Y. (2012). Five different piscidins from Nile tilapia, Oreochromis niloticus: analysis of their expressions and biological functions. PLoS One, 7(11), e50263.
Peters, B. M., Shirtliff, M. E., &; Jabra-Rizk, M. A. (2010). Antimicrobial peptides: primeval molecules or future drugs?. PLoS Pathog, 6(10), e1001067.
Phoenix, D. A., Dennison, S. R., &; Harris, F. (2013). Cationic Antimicrobial Peptides Antimicrobial Peptides (pp. 39-81): Wiley-VCH Verlag GmbH &; Co. KGaA.
Pinkse, M. W. H., Maier, C. S., Kim, J.-I., Oh, B.-H., &; Heck, A. J. R. (2003). Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry. Journal of Mass Spectrometry, 38(3), 315-320.
Piras, A., Sandreschi, S., Maisetta, G., Esin, S., Batoni, G., &; Chiellini, F. (2015). Chitosan Nanoparticles for the Linear Release of Model Cationic Peptide. Pharm Res, 1-7.
Ponti, D., Mignogna, G., Mangoni, M. L., De Biase, D., Simmaco, M., &; Barra, D. (1999). Expression and activity of cyclic and linear analogues of esculentin-1, an anti-microbial peptide from amphibian skin. Eur J Biochem, 263(3), 921-927.
Porter, D., Weremowicz, S., Chin, K., Seth, P., Keshaviah, A., Lahti-Domenici, J., Polyak, K. (2003). A neural survival factor is a candidate oncogene in breast cancer. Proceedings of the National Academy of Sciences, 100(19), 10931-10936.
Projan, S. J. (2003). Why is big Pharma getting out of antibacterial drug discovery? Current Opinion in Microbiology, 6(5), 427-430.
Pushpanathan, M., Rajendhran, J., Jayashree, S., Sundarakrishnan, B., Jayachandran, S., &; Gunasekaran, P. (2012). Identification of a novel antifungal peptide with chitin-binding property from marine metagenome. Protein Pept Lett, 19(12), 1289-1296.
Rad, R., Ballhorn, W., Voland, P., Eisenacher, K., Mages, J., Rad, L., Krug, A. (2009). Extracellular and intracellular pattern recognition receptors cooperate in the recognition of Helicobacter pylori. Gastroenterology, 136(7), 2247-2257.
Rad, R., Brenner, L., Bauer, S., Schwendy, S., Layland, L., da Costa, C. P., Prinz, C. (2006). CD25+/Foxp3+ T Cells Regulate Gastric Inflammation and Helicobacter pylori Colonization In vivo. Gastroenterology, 131(2), 525-537.
Rad, R., Brenner, L., Krug, A., Voland, P., Mages, J., Lang, R., Prinz, C. (2007). Toll-Like Receptor–Dependent Activation of Antigen-Presenting Cells Affects Adaptive Immunity to Helicobacter pylori. Gastroenterology, 133(1), 150-163.e153.
Rad, R., Gerhard, M., Lang, R., Schoniger, M., Rosch, T., Schepp, W., Prinz, C. (2002). The Helicobacter pylori blood group antigen-binding adhesin facilitates bacterial colonization and augments a nonspecific immune response. J Immunol, 168(6), 3033-3041.
Radzishevsky, I., Krugliak, M., Ginsburg, H., &; Mor, A. (2007). Antiplasmodial activity of lauryl-lysine oligomers. Antimicrobial Agents and Chemotherapy, 51(5), 1753-1759.
Raetz, C. R., &; Whitfield, C. (2002). Lipopolysaccharide endotoxins. Annu Rev Biochem, 71, 635-700.
Rassow, J. (2011). Helicobacter pylori vacuolating toxin A and apoptosis. Cell Commun Signal, 9, 26.
Rathbone, B. J., Wyatt, J. I., Worsley, B. W., Shires, S. E., Trejdosiewicz, L. K., Heatley, R. V., &; Losowsky, M. S. (1986). Systemic and local antibody responses to gastric Campylobacter pyloridis in non-ulcer dyspepsia. Gut, 27(6), 642-647.
Ricci, C., Holton, J., &; Vaira, D. (2007). Diagnosis of Helicobacter pylori: invasive and non-invasive tests.