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研究生:曹李宏
論文名稱:牛乳鐵蛋白對大腸桿菌與幽門螺旋桿菌抗菌作用之探討
論文名稱(外文):The antibiotic effect of bovine lactoferrin on Escherichia coli and Helicobacter pylori
指導教授:毛嘉洪
學位類別:碩士
校院名稱:國立中興大學
系所名稱:獸醫微生物學研究所
學門:獸醫學門
學類:獸醫學類
論文種類:學術論文
論文出版年:1999
畢業學年度:87
語文別:中文
論文頁數:66
中文關鍵詞:乳鐵蛋白大腸桿菌幽門螺旋桿菌
外文關鍵詞:lactoferrinEscherichia coliHelicobacter pylori
相關次數:
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本研究在分析乳鐵蛋白之抗菌能力,並探討其可能的抗菌機制。實驗結果顯示,乳鐵蛋白可有效的抑制引起仔豬嚴重下痢的大腸桿菌,亦可抑制引起胃、十二指腸潰瘍的幽門螺旋桿菌之生長。乳鐵蛋白濃度須達25 μM始有明顯抑制細菌生長的作用,若乳鐵蛋白濃度降低,此抑制細菌生長的作用也會逐漸消失,而乳鐵蛋白抑制細菌生長的作用可被環境中過量的鐵離子所終止。在實驗中並比較運鐵蛋白、儲鐵蛋白與乳鐵蛋白的抗菌能力,這些同樣可以與鐵離子結合的蛋白,均有抑制大腸桿菌生長之作用,也說明了乳鐵蛋白可透過與細菌競爭鐵離子而達到抑制細菌之作用。此外,在培養基加入大量死菌的情況下,乳鐵蛋白抑制細菌生長之作用也隨之消失,因而推論乳鐵蛋白亦可透過與細菌發生直接作用,而達到抑制細菌生長的功能。
Lactoferrin is an antimicrobial iron-binding glycoprotein, and the molecular weight is about 80 kDa. It is found in most mucous secretion of mammals including milk, saliva, tears, and released from activated neutrophil in the inflammatory response. The antibacterial activity and the possible mechanism of lactoferrin was studied. The results showed that lactoferrin could effectively inhibit the growth of 5 strains of E. coli that cause severe diarrhea of piglets, and 9 strains of H. pylori that cause gastrointestine disease. The effective dose of lactoferrin for antibacterial activity was 25M. We also found that this antibacterial effect would be blocked by excess of iron. In comparison of apo-transferrin, apo-ferritin, and lactoferrin showed similar activity of inhibition of E. coli. This comes to a conclusion that the inhibition effect is caused by the competition of iron in LB medium. Furthermore, we also found that in the surrounding of outer membrane from dead bacteria, the antibacterial activity of lactoferrin was diminished. Therefore we also believed that lactoferrin may act directly on the outer membrane to inhibit the gram negative bacteria growth.
第一章 緒言
第二章 文獻探討
第一節 乳鐵蛋白
第二節 Lactoferricin
第三節 幽門螺旋桿菌
第三章 材料與方法
第一節、菌種來源
第二節、細菌之培養
第三節、兩種乳鐵蛋白的比較
第四節、乳鐵蛋白對大腸桿菌生長之影響
第五節、乳鐵蛋白與抗生素抑菌作用之比較
第六節、鐵離子對乳鐵蛋白抑菌作用之影響
第七節、其他攜鐵蛋白與乳鐵蛋白的抑菌作用之比較
第八節、乳鐵蛋白與死大腸桿菌菌液的作用
第九節、乳鐵蛋白對幽門螺旋桿菌生長之影響
第四章 結果
第一節、細菌生長曲線之測定
第二節、乳鐵蛋白之比較
第三節、乳鐵蛋白對大腸桿菌生長之影響
第四節、乳鐵蛋白與抗生素抗菌作用之比較
第五節、鐵離子對乳鐵蛋白抑制大腸桿菌生長作用之影響
第六節、乳鐵蛋白與其他攜鐵蛋白對抑制大腸桿菌能力之比較
第七節、乳鐵蛋白與大腸桿菌外細胞膜的作用
第八節、乳鐵蛋白對幽門螺旋桿菌生長之影響
第五章、討論
第六章、結論
參考文獻
陳增興。1996。幽門螺旋桿菌。臨床醫學。38:83-90。
Anderson, B. F., H. M. Baker, G. E. Norris, D. W. Rice, and E. N. Baker. 1989. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8A resolution. J. Mol. Biol. 209:711-734.
Arnold, R. R., J. E. Russell, W. J. Champion, M. Brewer, and J. J. Gauthier. 1982. Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation. Infect. Immun. 35:792-799.
Arnold, R. R., M. F. Cole, and J. R. McGhee. 1977. A bactericidal effect for human lactoferrin. Science 197:263-265.
Bauerfeinf, P., R. Garner, B. E. Dunn, and H. L. T. Mobley. 1997. Synthesis and activity of Helicobacter pylori urease and catalase at low pH. Gut 40:25-30.
Bellamy, W., H. Wakabayashi, M. Takase, K. Kawase, S. Shimamura, and M. Tomita. 1993. Killing of Candida albicans by lactoferrin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol. 182:97-105.
Bellamy, W., M. Takase, H. Wakabayashi, K. Kawase, and M. Tomita. 1992. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 73:472-479.
Bellamy, W., M. Takase, K. Yamauchi, H. Wakabayashi, K. Kawase, and M. Tomita. 1992. Identification of the bactericidal domain of lactoferrin. Biomed. Biophys. Acta. 1121:130-136.
Britigan, B. E., J. S. Serody, M. B. Hayek, L. M. Charniga, and M. S. Cohen. 1991. Uptake of lactoferrin by mononuclear phagocytes inhibits their ability to form hydroxyl radical and protects them from membrane autoperoxidation. J. Immunol. 147:4271-4277.
Chapple, D.S., D. J. Mason, C. L. Joannou, E. W. Odell, V. Gant, and R. W. Evans. 1998. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111. Infect. Immun. 66:2423-2440.
Chmiela, M., E. Czkwianianc, T. Wadstrom, and W. Rudnicka. 1997. Role of Helicobacter pylori surface structures in bacterial interaction with macrophages. Gut 40:20-24.
Chou, C. H., B. Sheu, H. Yang, P. Cheng, J. Shin, C. Chen, and X. Lin. 1997. Clinical assessment of the bacterial load of Helicobacter pylori on gastric mucosa by a new multi-scaled rapid urease test. J. Gastroenterol. Hepatol. 12:1-6.
Cohen, M. S., J. Mao, G. T. Rasmussen, J. S. Serody, and B. E. Britigan. 1992. Interaction of lactoferrin and lipopolysaccharide (LPS): effects on the antioxidant property of lactoferrin and the ability of LPS to prime human neutrophils for enhanced superoxide formation. J. Infect. Dis. 166:1375-1378.
Dhaenens, L., F. Szczebara, and M. O. Husson. 1997. Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori. Infect. Immun. 65:514-518.
Dionysius, D. A., and J. M. Milne. 1997. Antibacterial peptide of bovine lactoferrin: purificayion and characterization. J. Dairy Sci. 80:667-674.
Eck, M., B. Schmauer, R. Haas, A. Greiner, S. Czub and H. K. Muller-Hermelink. 1997. Malt-type lymphoma of the stomach is associated with Helicobacter pylori strains expressing the CagA protein. Gastroenterology 112:1482-1486.
Elass-Rochard, E., A. Roseanu, D. Legrand, M. Trif, V. Salmon, C. Motas, J. Montreuil, and G. Spik. 1995. Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli O55B5 lipopolysaccharide. Biochem. J. 312:839-845.
Elliot, J. I., B. Senft, G. Erhardt, and D. Fraser. 1984. Isolation of lactoferrin and its concentration in sow’s colostrum and milk during a 21-day lactation. J. Anim. Sci. 59:1080-1084.
Ellison III, R. T., and T. J. Giehl. 1991. Killing of gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest.. 88:1080-1091.
Ellison III, R. T., T. J. Giehl, and F. M. Laforce. 1988. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2781.
El-Zaatari, F. A. K., J. S. Woo, A. Badr, M. S. Osato, H. Serna, L. M. Lichtemberger, R. M. Genta, and D. Y. Graham. 1997. Failure to isolate Helicobacter pylori from stray cats indicates that H. pylori in cats may be an anthroponsis - an animal infection with a human pathogen. J. Med. Microbiol. 46:372-376.
Ferrero, R. L., J. Thiberge, and A. Labigne. 1997. Local immunoglobulin G antibodies in the stomach may contribute to immunity against Helicobacter infection in mice. Gastroenterology 113:185-194.
Fujihara, T., and K. Hayashi. 1995. Lactoferrin inhibits herpes simplex virus type-1 (HSV-1) infection to mouse cornea. Arch. Virol. 140:1469-1472.
Gado, I., J. Erdei, V. G. Laszlo, J. Paszti, E. Czirok, T. Kontrohr, I. Toth, A. Forsgren, and A. S. Naidu. 1991. Correlation between human lactoferrin binding protein and colicin susceptibility in Escherichia coli. Antimicrob. Agen. Chemother. 35:2538-2543.
Ghiara, P., M. Marchetti, M. J. Blaser, M. K. R. Tummuru, T. L. Cover, E. D. Segal, L. S. Tompkins, and R. Rappuoli. 1995. Role of the Helicobacter pylori virulence factors vacuolatiog cytotoxin, CagA, and urease in a mouse model of disease. Infect. Immun. 63:4154-4160.
Goodwin, C. S., J. A. Armstrong, T. Chilvers, M. Peters, M. D. collins, L. Sly, W. McConnell, and W. E. S. Harper. 1989. Transfer of Campylobacter pyloris and Campylobacter mustelae to Helicobacter gen. Nov. as Helicobacetr pylori comb. Nov. and Helicobacter mustelae comb. Nov. , respectively. J. Sys. Bacteriol. 39:397-405.
Grover, M., O. Giouzeppos, R. D. Schnagl, and J. T. May. 1997. Effect of human milk prostaglandins and lactoferrin on respiratory syncytial virus and rotavirus. Acta. Paediatr. 86:315-316.
Hansen, N. E., J. Malmquist, and J. Thorell. 1975. Plsma myelo-peroxidase and lactoferrin measured by radioimmunoassay: relation to neutrophil kinetics. Acta. Med. Scand. 198:437-443.
Harmsen, M. C., P. J. Swart, M. P. De Bethune, R. Pauweles, E. De Clercq, T. H. The, and D. K. Meijer. 1995. Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J. Infect. Dis. 172:380-388.
Hoek, K. S., J. M. Milne, P. A. Grieve, and D. A. Dionysius. 1997. Antibacterial activity of bovine lactoferrin-derived peptides. Antimicrob. Agen. Chemother. 41:54-59.
Hwang, P. M., N. Zhou, X. Shan, C. H. Arrowsmith, and H. J. Vogel. 1998. Three-dimensional solution structure of lactoferrin B, an antimicrobial peptide derived from bovine lactoferrin. Biochem. 37: 4288-4298.
Isanida, T., T. Tanaka, Y. Omata, K. Yamauchi, K. Shimazaki, and A. Saito. 1998. Protective effect of lactoferrin against Toxoplasma gondii infection in mice. J. Vet. Med. Sci. 60:241-244.
Kang, J. H., M. K. Lee, K. L. Kim, and K. S. Hahm. 1996. Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Protein Res. 48:357-363.
Kuwata, H., T. T. Yip, C. L. Yip, M. Tomita, and T. W. Hutchens. 1998. Bactericidal domain of lactoferrin: detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry. Biochem. Biophys. Res. Commun. 245:764-773.
Laforce, F. M., D. S. Bosse, and R. T. Ellison III. 1986. Effect of aerosolized Escherichia coli and Stapylococcus aureus on iron and iron-binding protein in lung lavage fluid. J. Infect. Dis. 154:959-965.
Lee, A., J. O''rouoke, M. C. D. Ungria, B. Robertson, G. Daskalopoulos, and M. F. Sixon. 1997. A standardized mouse model of Helicobscter pylori infection: introducing the Sydney strain. Gastroenterology 112:1386-1397.
Lima, M. F., and F. Kierszenbaum. 1985. Lactoferrin effects on phagocytic cell function: I. Increased uptake and killing of an intracellular parasie by murine macrophages and human monocytes. J. Immunol. 134:4176-4183.
Lima, M. F., and F. Kierszenbaum. 1987. Lactoferrin effects on phagocytic cell function: I. The presence of iron is required for the lactoferrin molecule to stimulate intracellular killing by macrophages but not to enhance the uptake of particles and microorganisms. J. Immunol. 139:1647-1651.
Longhi, C., M. P. Conte, W. Bellamy, L. Segamti, and P. Valenti. 1994. Effect of lactoferrin B, a pepsin-generated peptide of bovine lactoferrin, on Escherichia coli HB101(pRI302) entry Hela cells. Med. Microbiol. Immunol. 183:77-85.
Lonnerdal, B., E. Forsum, M. Gebre-Medhin, and L. Hambraeus. 1976. Breast milk composition in Ethiopian and Swedish mothers. II. Lactose, nitrogen, and protein contents. Am. J. Clin. Nutr. 29:1134-1141.
Marshall, B., and J. R. Warren. 1983. Unidentified curved bacillus on gastric epithelium in active chronic gastritis. Lancet 1:1273-1275.
Martin-De-Argila, C., D. Boixeda, C. Redondo, I. Alvarez, J. P. Gisbert, A. G. Plaza and R. Canton. 1997. Relation between histologic subtypes and lacation of gastric cancer and Helicobacter pylori. Scand. J. Gastroenterol. 32:303-307.
Mason, D. J., Chapple D. S., Joannou C. L., Odell E. W., Gant V., and Evans R. W. 1998. Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111. Infect. Immun. 66:2434-2400.
Masson, P. L., J. F. Heremans, and C. Dive., 1966. An iron-binding protein common to many external secretions. Clin. Chem. Acta. 13:735-739.
Masson, P. L., J. F. Heremans, and E. Schonne. 1969. Lactoferrin, and iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 130:643-658.
Metz-Boutigue, M. H., J. Jolles, J. Mazurier, F. Schoentgen, D. Legrand, G. Spik, J. Montreuil, and P. Jolles. 1984. Human lactotrasferrin: amino acid sequence and structural comparison with other transferrins. Eur. J. Biochem. 145:659-676.
Miehlke, S., R. Reddy, M. S. Osato, P. P. Ward, O. M. Conneely, and D. Y. Graham. 1996. Direct activity of recombinant human lactoferrin against Helicobacter pylori. J. Clin. Microbiol. 34:2593-2594.
Moran, A. P. 1996. Pathogenic properties of Helicobacter pylori. Scan. J. Gastroenterol. 31 suppl. 215:22-31.
Mossi, S., B. M. Wyss, E. L. Renner, H. S. Merki, G. Gamboni, and C. Beglinger. 1993. Influence of Helicobacter pylori, sex, age on serum gastrin and pepsinogen concentrations in subjects without symptoms and patients with dudenal ulcers. Gut 34:752-756.
Murakita, H., M. Hirai, S. Ito, T. Azuma, T. Kato, Y. Kohli, and M. Kuritama. 1996. Cytotoxin and urease activities of Helicobacter pylori isolates from Japanese patients with atropic gastritis and dudenal ulcer. J. Gastroenterol. 11:819-824.
Naidu, S. S., U. Svensson, A. R. Kishore, and A. S. Naidu. 1993. Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurine. Antimicrob. Agen. Chemother. 37: 240-245.
Nakao, K., I. Imoto, E. C. Gabazza, K. Yamauchi, N. Yamazaki, Y. Taguchi, T. Shibata, S. Takaji, N. Ikemura, and M. Misaki. 1997. Gastric juice levels of lactoferrin and Helicobacter pylori infection. Scand. J. Gastroenterol. 32:530-534.
Nakao, K., I. Imoto, K. Yamauchi, N. Yamazaki, Y. Taguchi, T. Shibata, S. Takaji, N. Ikemura, and M. Misaki. 1997. Relation of lactoferrin levels in gastric mucosa with Helicobacter pylori infection and with the degree of gastric inflammation. Amer. J. Gastroenterol. 92:1005-1011.
O’Rourke, J., A, Lee, and J. G. Fox. 1992. An ultrastructural study of Helicobacter mustelae and evidence of a specific association of a gastric mucosa. J. Med. Microbiol. 36:420-427.
Odell, E. W., R. Sarra, M. Foxworthy, D. S. Chapple, and R. W. Evans. 1996. Antibacterial activity of peptides homologous to a loop region in human lactoferrin. FEBS Lett. 382:175-178.
Osaki, T., H. Yamaguchi, H. Taguchi, J. Kumada, S. Ogata, and S. Kamiya. 1997. Studies on the relationship between adhesive activity and haemagglutination by Helicobacter pylori. J. Med. Microbiol. 46:117-121.
Palma, C., A. Cassone, D. Serbousek, C. A. Pearson, and J. Y. Djeu. 1992. Lactoferrin release and interleukin-1, interleukin-6, and tumor necrosis factor production by human polymorphonuclear cells stimulated by various lipopolysaccharides: relationship to growth inhibition of Candida albicans. Infect. Immun. 60:4606-4611.
Parsonnet, J., G. D. Friedman, N. Orentreich, and H. Vogelman. 1997. Risk for gastric cancer in people with CagA positive or CagA negtive Helicobacter pulori infection. Gut 40:297-301.
Piccolomini, R., G. D. Bonaventura, D. Festi, G. Catamo, F. Laterza, and M. Neri. 1997. Optimal combination of media for primary isolation of Helicobacter pylori from gastric biopsy specimens. J. Clin. Microbiol. 35:1541-1544.
Reilly, T. G., V. Poxon, D. S. A. Sanders, T. S. J. Elliott, and R. P. Walt. 1997. Comparison of serum, salivary, and rapid whole blood diagnostic tests for Helicobacter pylori and their validation against endoscopy based tests. Gut 40:454-458.
Ricci, V., C. Ciacci, R. Zarrilli, P. Sommi, M. K. R. Tummuru, C. D. V. Blanco, C. B. Bruni, T. L. Cover, M. J. Blaser, and M. Romano. 1996. Effect of Helicobacter pylori on gastric epithelial cell migration and proliferation in vitro: role of VacA and CagA. Infect. Immun. 64:2829-2833.
Roberts, A. K., R. Chierici, G. Sawatzki, M. J. Hill, S. Volpato, and V. Vigi. 1992. Supplementation of an adapted formula with bovine lactoferrin: 1. Effect on the infant faecal flora. Acta. Paediatr. 81:119-24.
Schanbacher, F. L., and K. L. Smith. 1975. Formation and role of unusual whey proteins and enzymes: Relation to mammary function. J. Dairy Sci. 58:1048-1062.
Shimazaki, K. I., M. S. Nam, S. Harakawa, T. Tanaka, Y. Omata, A. Saito, H. Kumura, K. Mikawa, I. Igarashi, and N. Suzuki. 1996. Monoclonal antibody against bovine lactoferricin and its epitopic site. J. Vet. Med. Sci. 58:1227-1229.
Skerlavaj, B., D. Romeo, and R. Gennaro. 1990. Rapid membrane permeabilization of vial functions of gram-negative bacteria by bactenecins. Infec. Immun. 58:3724-3730.
Soukka, T., M. Lumikari, and J. Tenovuo. 1991. Combination inhibitory effect of lactoferrin and lactoperoxidase system on the viability of Streptococcus mutans, serotype C. Scand. J. Dent. Res. 99:390-396.
Tanaka, T., Y. Omata, A. Saito, K. Shimazaki, K. Yamauchi, M. Takase, K. Kawase, I. Igarashi, and N. Suzuki. 1995. Toxoplasma gondii: parasiticidal effects of bovine lactoferricin against parasites. Exp. Parasitol. 81:614-617.
Tomita, M, M. Takase, H. Wakabayashi, and W. Bellamy. 1994. Antibacterial peptides of lactoferrin. Advance. Exp. Med. Biol. 357:209-218.
Tomita, M., W. Bellamy, M. Takase, K. Yamauchi, H. Wahabayashi, and K. Kawase. 1991. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J. Dairy Sci. 74:4137-4142.
Tummuru, M. K. R., T. L. Cover, and M. J. Blaser. 1994. Mutation of the Cytotoxin-assiciated cagA gene does not affect the vacuolating cytotoxin activity of Helicobacter pylori. Infect. Immun. 62:2609-2613.
Van Der Hulst, R. W. M., A. V. D. Ende, F. W. Dekker, F. J. W. T. Kate, J. F. L. Weel, J. J. Keller, S. P. Kruizinga, J. Dankert, and G. N. J. Tytgat. 1997. Effect of Helicobacter pylori eradication on gastritis in relation to cagA: a prospective 1-year follow-up study. Gastroenterology 113:25-30.
Visca, P., C. Dalmastri, D. Verzili, G. Antonini, E. Chiancone, and P. Valenti. 1990. Interaction of lactoferrin with Escherichia coli cells and correlation with antibacterial activity. Med. Microbiol. Immunol. 179:323-333.
Wakabayashi, H., S. Abe, T. Okutomi, S. Tansho, K. Kawase and H. Yamaguchi. 1996. Cooperative anti-candida effects of lactoferrin or its peptides in combination with azole antifungal agents. Microbiol. Immunol. 40:821-825.
Xiang, Z., S. Censini, P. F. Bayeli, J. L. Telford, N. Figura, R. Rappuoli, and A. Covacci. 1995. Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin. Infect. Immun. 63:94-98.
Yamauchi, K., M. Tomita, T. J. Giehl, and R. T. Ellison III. 1993. Antibacterial activity of lactoferrin and pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
Yoo, Y. C., R. Watanabe, Y. Koike, M. Mitobe, K. Shimazaki, S. Watanabe, and I. Azuma. 1997. Apoptpis in human leukemic cells induced by lactoferricin, a bovine milk protein-derived peptide: involvement of reactive oxygen species. Biochem. Biophys. Res. Commun. 237:624-628.
Yoo, Y. C., S. Watanabe, R. Watanabe, K. Hata, K. Shimazaki, and I. Azuma. 1997. Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice. Jap. J. Cancer Res. 88:184-190.
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