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研究生:陳姿雁
研究生(外文):Zih-Yan Chen
論文名稱:薑黃素於抑制A型流感病毒之機制
論文名稱(外文):A mechanism of curcumin on anti-influenza A virus infection
指導教授:王孟亮
指導教授(外文):Ming-Liang Wong
學位類別:碩士
校院名稱:國立中興大學
系所名稱:獸醫學系暨研究所
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:2010
畢業學年度:98
語文別:中文
論文頁數:56
中文關鍵詞:流行性感冒病毒薑黃素紅血球凝集素抑制
外文關鍵詞:influenza viruscurcuminInhibition of haemagglutination
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薑黃素(curcumin)為薑黃萃取物,已經證明具有透過調節細胞訊息達到抗炎症、抗氧化、抗癌症的特性,其中也包含流感病毒複製所必需的NF-kappaB路徑。根據實驗室之前的發現,薑黃素能夠有效的抑制流感病毒的複製,且具有干擾血球凝集的作用,本論文的研究關注於探討薑黃素抗流感病毒的機制。研究結果顯果示薑黃素能減少感染流感病毒293T細胞的NF-kappaB活性。薑黃素也會降低流感病毒病毒斑的數量,卻不會影響非封套病毒如:腸病毒71型病毒斑的數量。根據之前科學的研究,透過固態核磁共振的觀察,薑黃素能鑲嵌在微脂體脂雙層膜上,因此我們假設薑黃素或許可透過與膜作用破壞封套病毒來干擾病毒的進入。我們以包裹螢光物質(sulforhodamine B)的微脂體模擬封套結構,薑黃素處理後造成微脂體的螢光物質從微脂體釋出,且此效應可藉由加入流感病毒反轉,這暗示薑黃素可能會影響封套的完整性。總合來說薑黃素可能的抗流感病毒機制之一為藉由影響病毒封套和封套上與感染有關的HA蛋白質,但這二個機制是各自獨立運作或是彼此影響仍需要進步探討。

Curcumin (a natural compound from curry) has been shown to exert anti-inflammatory, antioxidant, and anticarcinogenesis properties, acting through modulation of signal transduction pathways including NF-kappaB, required for efficient replication of influenza virus. Extending from our previous observation that treatment of curcumin efficiently blocked influenza replication and haemagglutination (HA) activity, the goal of present study focuses on investigation of the mechanism of anti-influenza activity mediated by curcumin. The result indicated that curcumin treatment decreased NF-kappaB activity elevated by LPS or influenza virus infection in 293T cell. Surprisingly, in addition to influenza virus, the plaque formation ability of all enveloped viruses analyzed, but not that of non-enveloped virus, i.e. EV71enterovirus 71, was also blocked by curcumin. As revealed by solid state NMR experiment, curcumin inserts deeply into the membrane in a transbilayer orientation, we hypothesis that curcumin might associate with membrane structure leading to disruption of virus envelop which in tern interferes virus entry. The impact of curcumin on membrane was then tested by fluorescent dye (Sulforhodamine sulforhodamine B) packed liposome particles mimicking envelope structure. Curcumin treatment caused the leakage of Ssulforhodamine B from liposome, and this effect was reverted by addition of influenza viruses, indicating that curcumin might affect the integrity of envelop structure. Taken together, the anti-influenza virus activity of curcumin might act through affecting viral envelop and the function of HA, the envelop protein; whether these two events work independently or act in concert requires further investigation.

中文摘要 I
ABSTRACT II
目次 III
圖次 V
緒言 1

第一章 文獻探討 3
第一節 流行性感冒之爆發史 3
第二節 流行性感冒病毒 4
第三節 流感病毒結構與功能 4
第四節 流感病毒生活史 (圖二) 8
第五節 抗流感病毒藥物 10
第六節 薑黃素(CURCUMINCURCUMIN) 13
第七節 NF-ΚB路徑與流感病毒感染之相關研究 16
第八節 研究動機與方向 17
第二章 材料與方法 18
第一節 實驗材料以及基本實驗步驟 18
第二節 重要實驗設計與步驟 22
第三章 結果 26
第一節 以報導基因表現探討CURCUMINCURCUMIN抗病毒機制: NF- KB路徑 26
第二節 測試CURCUMIN類似物有無抗病毒功能 26
第三節 CURCUMIN抗病毒的細胞外源性路徑 27
第四節 比較CURCCUMIN對於PR8和PRV的抗病毒效力 29
第五節 CURUCUMIN抑制病毒功能反轉實驗 29
第四章 討論 31
參考文獻 45


陳大元。(2008) 薑黃素抗流感的能力。國立中興大學獸醫系碩士畢業論文
Aggarwal, B.B., Kumar, A., and Bharti, A.C. (2003). Anticancer potential of curcumin: preclinical and clinical studies. Anticancer Res 23, 363-398.
Akarsu, H., Burmeister, W.P., Petosa, C., Petit, I., Muller, C.W., Ruigrok, R.W., and Baudin, F. (2003). Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J 22, 4646-4655.
Alexopoulou, L., Holt, A.C., Medzhitov, R., and Flavell, R.A. (2001). Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 413, 732-738.
Ammon, H.P., and Wahl, M.A. (1991). Pharmacology of Curcuma longa. Planta Med 57, 1-7.
Andrejeva, J., Childs, K.S., Young, D.F., Carlos, T.S., Stock, N., Goodbourn, S., and Randall, R.E. (2004). The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. Proc Natl Acad Sci U S A 101, 17264-17269.
Barry, J., Fritz, M., Brender, J.R., Smith, P.E., Lee, D.K., and Ramamoorthy, A. (2009). Determining the effects of lipophilic drugs on membrane structure by solid-state NMR spectroscopy: the case of the antioxidant curcumin. J Am Chem Soc 131, 4490-4498.
Bhaumik, S., Jyothi, M.D., and Khar, A. (2000). Differential modulation of nitric oxide production by curcumin in host macrophages and NK cells. FEBS Lett 483, 78-82.
Bonizzi, G., and Karin, M. (2004). The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol 25, 280-288.
Booy, F.P., Ruigrok, R.W., and van Bruggen, E.F. (1985). Electron microscopy of influenza virus. A comparison of negatively stained and ice-embedded particles. J Mol Biol 184, 667-676.
Bouamama, H., Villard, J., Benharref, A., and Jana, M. (1999). Antibacterial and antifungal activities of Cistus incanus and C. monspeliensis leaf extracts. Therapie 54, 731-733.
Bright, R.A., Medina, M.J., Xu, X., Perez-Oronoz, G., Wallis, T.R., Davis, X.M., Povinelli, L., Cox, N.J., and Klimov, A.I. (2005). Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: a cause for concern. Lancet 366, 1175-1181.
Briolant, S., Garin, D., Scaramozzino, N., Jouan, A., and Crance, J.M. (2004). In vitro inhibition of Chikungunya and Semliki Forest viruses replication by antiviral compounds: synergistic effect of interferon-alpha and ribavirin combination. Antiviral Res 61, 111-117.
Bui, M., Whittaker, G., and Helenius, A. (1996). Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J Virol 70, 8391-8401.
Bui, M., Wills, E.G., Helenius, A., and Whittaker, G.R. (2000). Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J Virol 74, 1781-1786.
Caton, A.J., and Robertson, J.S. (1980). Structure of the host-derived sequences present at the 5'' ends of influenza virus mRNA. Nucleic Acids Res 8, 2591-2603.
Chase, G., Deng, T., Fodor, E., Leung, B.W., Mayer, D., Schwemmle, M., and Brownlee, G. (2008). Hsp90 inhibitors reduce influenza virus replication in cell culture. Virology 377, 431-439.
Chen, D.-Y. (2008). the effect of curcumin on anti-flu avtivities. In graduate institute of veterinary public health (taichung, national chung hsing university).
Chu, W.M., Ostertag, D., Li, Z.W., Chang, L., Chen, Y., Hu, Y., Williams, B., Perrault, J., and Karin, M. (1999). JNK2 and IKKbeta are required for activating the innate response to viral infection. Immunity 11, 721-731.
Cinatl, J., Morgenstern, B., Bauer, G., Chandra, P., Rabenau, H., and Doerr, H.W. (2003). Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus. Lancet 361, 2045-2046.
Corson, T.W., and Crews, C.M. (2007). Molecular understanding and modern application of traditional medicines: triumphs and trials. Cell 130, 769-774.
Crance, J.M., Scaramozzino, N., Jouan, A., and Garin, D. (2003). Interferon, ribavirin, 6-azauridine and glycyrrhizin: antiviral compounds active against pathogenic flaviviruses. Antiviral Res 58, 73-79.
Davies, W.L., Grunert, R.R., Haff, R.F., McGahen, J.W., Neumayer, E.M., Paulshock, M., Watts, J.C., Wood, T.R., Hermann, E.C., and Hoffmann, C.E. (1964). Antiviral Activity of 1-Adamantanamine (Amantadine). Science 144, 862-863.
De Clercq, E. (2006). Antiviral agents active against influenza A viruses. Nat Rev Drug Discov 5, 1015-1025.
Droebner, K., Ehrhardt, C., Poetter, A., Ludwig, S., and Planz, O. (2007). CYSTUS052, a polyphenol-rich plant extract, exerts anti-influenza virus activity in mice. Antiviral Res 76, 1-10.
Dutta, K., Ghosh, D., and Basu, A. (2009). Curcumin protects neuronal cells from Japanese encephalitis virus-mediated cell death and also inhibits infective viral particle formation by dysregulation of ubiquitin-proteasome system. J Neuroimmune Pharmacol 4, 328-337.
Ehrhardt, C., Marjuki, H., Wolff, T., Nurnberg, B., Planz, O., Pleschka, S., and Ludwig, S. (2006). Bivalent role of the phosphatidylinositol-3-kinase (PI3K) during influenza virus infection and host cell defence. Cell Microbiol 8, 1336-1348.
Elford, W.J., and Galloway, I.A. (1936). The Size of the Virus of Aujeszky''s Disease ("Pseudo-rabies", "Infectious Bulbar Paralysis", "Mad-itch") by Ultrafiltration Analysis. J Hyg (Lond) 36, 536-539.
Flory, E., Kunz, M., Scheller, C., Jassoy, C., Stauber, R., Rapp, U.R., and Ludwig, S. (2000). Influenza virus-induced NF-kappaB-dependent gene expression is mediated by overexpression of viral proteins and involves oxidative radicals and activation of IkappaB kinase. J Biol Chem 275, 8307-8314.
Garcia-Sastre, A., Egorov, A., Matassov, D., Brandt, S., Levy, D.E., Durbin, J.E., Palese, P., and Muster, T. (1998). Influenza A virus lacking the NS1 gene replicates in interferon-deficient systems. Virology 252, 324-330.
Glaser, L., Stevens, J., Zamarin, D., Wilson, I.A., Garcia-Sastre, A., Tumpey, T.M., Basler, C.F., Taubenberger, J.K., and Palese, P. (2005). A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity. J Virol 79, 11533-11536.
Gorlich, D., and Kutay, U. (1999). Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 15, 607-660.
Goto, H., and Kawaoka, Y. (1998). A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc Natl Acad Sci U S A 95, 10224-10228.
Govorkova, E.A., Ilyushina, N.A., Boltz, D.A., Douglas, A., Yilmaz, N., and Webster, R.G. (2007). Efficacy of oseltamivir therapy in ferrets inoculated with different clades of H5N1 influenza virus. Antimicrob Agents Chemother 51, 1414-1424.
Hampson, A.W., and Mackenzie, J.S. (2006). The influenza viruses. Med J Aust 185, S39-43.
Han, S.S., Chung, S.T., Robertson, D.A., Ranjan, D., and Bondada, S. (1999). Curcumin causes the growth arrest and apoptosis of B cell lymphoma by downregulation of egr-1, c-myc, bcl-XL, NF-kappa B, and p53. Clin Immunol 93, 152-161.
He, X., Zhou, J., Bartlam, M., Zhang, R., Ma, J., Lou, Z., Li, X., Li, J., Joachimiak, A., Zeng, Z., et al. (2008). Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus. Nature 454, 1123-1126.
Herlocher, M.L., Carr, J., Ives, J., Elias, S., Truscon, R., Roberts, N., and Monto, A.S. (2002). Influenza virus carrying an R292K mutation in the neuraminidase gene is not transmitted in ferrets. Antiviral Res 54, 99-111.
Hiscott, J. (2001). Introduction--cytokine receptors, signaling pathways and viruses. Cytokine Growth Factor Rev 12, 129-131.
Hoever, G., Baltina, L., Michaelis, M., Kondratenko, R., Tolstikov, G.A., Doerr, H.W., and Cinatl, J., Jr. (2005). Antiviral activity of glycyrrhizic acid derivatives against SARS-coronavirus. J Med Chem 48, 1256-1259.
Holmes, E.C., Lipman, D.J., Zamarin, D., and Yewdell, J.W. (2006). Comment on "Large-scale sequence analysis of avian influenza isolates". Science 313, 1573; author reply 1573.
Horimoto, T., and Kawaoka, Y. (1995). The hemagglutinin cleavability of a virulent avian influenza virus by subtilisin-like endoproteases is influenced by the amino acid immediately downstream of the cleavage site. Virology 210, 466-470.
Huang, T.S., Palese, P., and Krystal, M. (1990). Determination of influenza virus proteins required for genome replication. J Virol 64, 5669-5673.
Hung, W.C., Chen, F.Y., Lee, C.C., Sun, Y., Lee, M.T., and Huang, H.W. (2008). Membrane-thinning effect of curcumin. Biophys J 94, 4331-4338.
Ishihama, A., Mizumoto, K., Kawakami, K., Kato, A., and Honda, A. (1986). Proofreading function associated with the RNA-dependent RNA polymerase from influenza virus. J Biol Chem 261, 10417-10421.
Ito, T., Suzuki, Y., Suzuki, T., Takada, A., Horimoto, T., Wells, K., Kida, H., Otsuki, K., Kiso, M., Ishida, H., et al. (2000). Recognition of N-glycolylneuraminic acid linked to galactose by the alpha2,3 linkage is associated with intestinal replication of influenza A virus in ducks. J Virol 74, 9300-9305.
Itoh, Y., Shinya, K., Kiso, M., Watanabe, T., Sakoda, Y., Hatta, M., Muramoto, Y., Tamura, D., Sakai-Tagawa, Y., Noda, T., et al. (2009). In vitro and in vivo characterization of new swine-origin H1N1 influenza viruses. Nature 460, 1021-1025.
Ives, J.A., Carr, J.A., Mendel, D.B., Tai, C.Y., Lambkin, R., Kelly, L., Oxford, J.S., Hayden, F.G., and Roberts, N.A. (2002). The H274Y mutation in the influenza A/H1N1 neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo. Antiviral Res 55, 307-317.
Jayaprakasha, G.K., Jagan Mohan Rao, L., and Sakariah, K.K. (2002). Improved HPLC method for the determination of curcumin, demethoxycurcumin, and bisdemethoxycurcumin. J Agric Food Chem 50, 3668-3672.
Jing, X., Ma, C., Ohigashi, Y., Oliveira, F.A., Jardetzky, T.S., Pinto, L.H., and Lamb, R.A. (2008). Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel. Proc Natl Acad Sci U S A 105, 10967-10972.
Karin, M., and Delhase, M. (2000). The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling. Semin Immunol 12, 85-98.
Kim, C.U., Lew, W., Williams, M.A., Liu, H., Zhang, L., Swaminathan, S., Bischofberger, N., Chen, M.S., Mendel, D.B., Tai, C.Y., et al. (1997). Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J Am Chem Soc 119, 681-690.
Knipe, D.M., and Howley, P.M. (2007). Field''s Virology, 5th edn (Lippincott Williams & Wilkins ).
Krug, R.M., Yuan, W., Noah, D.L., and Latham, A.G. (2003). Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein. Virology 309, 181-189.
Kumar, N., Xin, Z.T., Liang, Y., and Ly, H. (2008). NF-kappaB signaling differentially regulates influenza virus RNA synthesis. J Virol 82, 9880-9889.
Kutluay, S.B., Doroghazi, J., Roemer, M.E., and Triezenberg, S.J. (2008). Curcumin inhibits herpes simplex virus immediate-early gene expression by a mechanism independent of p300/CBP histone acetyltransferase activity. Virology 373, 239-247.
Lam, A.Y., and Chung, Y. (2008). Establishing an on-site influenza vaccination service in an assisted-living facility. J Am Pharm Assoc (2003) 48, 758-763.
Le, Q.M., Kiso, M., Someya, K., Sakai, Y.T., Nguyen, T.H., Nguyen, K.H., Pham, N.D., Ngyen, H.H., Yamada, S., Muramoto, Y., et al. (2005). Avian flu: isolation of drug-resistant H5N1 virus. Nature 437, 1108.
Lee, J., Im, Y.H., Jung, H.H., Kim, J.H., Park, J.O., Kim, K., Kim, W.S., Ahn, J.S., Jung, C.W., Park, Y.S., et al. (2005a). Curcumin inhibits interferon-alpha induced NF-kappaB and COX-2 in human A549 non-small cell lung cancer cells. Biochem Biophys Res Commun 334, 313-318.
Lee, K.W., Kim, J.H., Lee, H.J., and Surh, Y.J. (2005b). Curcumin inhibits phorbol ester-induced up-regulation of cyclooxygenase-2 and matrix metalloproteinase-9 by blocking ERK1/2 phosphorylation and NF-kappaB transcriptional activity in MCF10A human breast epithelial cells. Antioxid Redox Signal 7, 1612-1620.
Lin, J.K., Pan, M.H., and Lin-Shiau, S.Y. (2000). Recent studies on the biofunctions and biotransformations of curcumin. Biofactors 13, 153-158.
Liptay, S., Weber, C.K., Ludwig, L., Wagner, M., Adler, G., and Schmid, R.M. (2003). Mitogenic and antiapoptotic role of constitutive NF-kappaB/Rel activity in pancreatic cancer. Int J Cancer 105, 735-746.
Liu, Y., Lou, Z., Bartlam, M., and Rao, Z. (2009). Structure-function studies of the influenza virus RNA polymerase PA subunit. Sci China C Life Sci 52, 450-458.
Ludwig, S., Pleschka, S., Planz, O., and Wolff, T. (2006). Ringing the alarm bells: signalling and apoptosis in influenza virus infected cells. Cell Microbiol 8, 375-386.
Lund, J.M., Alexopoulou, L., Sato, A., Karow, M., Adams, N.C., Gale, N.W., Iwasaki, A., and Flavell, R.A. (2004). Recognition of single-stranded RNA viruses by Toll-like receptor 7. Proc Natl Acad Sci U S A 101, 5598-5603.
Lundbaek, J.A. (2008). Lipid bilayer-mediated regulation of ion channel function by amphiphilic drugs. J Gen Physiol 131, 421-429.
Macken, C.A., Webby, R.J., and Bruno, W.J. (2006). Genotype turnover by reassortment of replication complex genes from avian influenza A virus. J Gen Virol 87, 2803-2815.
Mazur, I., Wurzer, W.J., Ehrhardt, C., Pleschka, S., Puthavathana, P., Silberzahn, T., Wolff, T., Planz, O., and Ludwig, S. (2007). Acetylsalicylic acid (ASA) blocks influenza virus propagation via its NF-kappaB-inhibiting activity. Cell Microbiol 9, 1683-1694.
Melen, K., Kinnunen, L., Fagerlund, R., Ikonen, N., Twu, K.Y., Krug, R.M., and Julkunen, I. (2007). Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes. J Virol 81, 5995-6006.
Min, J.Y., and Krug, R.M. (2006). The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2''-5'' oligo (A) synthetase/RNase L pathway. Proc Natl Acad Sci U S A 103, 7100-7105.
Naffakh, N., Massin, P., and van der Werf, S. (2001). The transcription/replication activity of the polymerase of influenza A viruses is not correlated with the level of proteolysis induced by the PA subunit. Virology 285, 244-252.
Nayak, D.P., Balogun, R.A., Yamada, H., Zhou, Z.H., and Barman, S. (2009). Influenza virus morphogenesis and budding. Virus Res 143, 147-161.
Nayak, D.P., Hui, E.K., and Barman, S. (2004). Assembly and budding of influenza virus. Virus Res 106, 147-165.
Neumann, G., Castrucci, M.R., and Kawaoka, Y. (1997). Nuclear import and export of influenza virus nucleoprotein. J Virol 71, 9690-9700.
Nicholls, H. (2006). Pandemic influenza: the inside story. PLoS Biol 4, e50.
Nichols, J.E., Niles, J.A., and Roberts, N.J., Jr. (2001). Human lymphocyte apoptosis after exposure to influenza A virus. J Virol 75, 5921-5929.
Nimmerjahn, F., Dudziak, D., Dirmeier, U., Hobom, G., Riedel, A., Schlee, M., Staudt, L.M., Rosenwald, A., Behrends, U., Bornkamm, G.W., et al. (2004). Active NF-kappaB signalling is a prerequisite for influenza virus infection. J Gen Virol 85, 2347-2356.
Noah, D.L., and Krug, R.M. (2005). Influenza virus virulence and its molecular determinants. Adv Virus Res 65, 121-145.
Obayashi, E., Yoshida, H., Kawai, F., Shibayama, N., Kawaguchi, A., Nagata, K., Tame, J.R., and Park, S.Y. (2008). The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature 454, 1127-1131.
Ohuchi, M., Asaoka, N., Sakai, T., and Ohuchi, R. (2006). Roles of neuraminidase in the initial stage of influenza virus infection. Microbes Infect 8, 1287-1293.
Onose, A., Hashimoto, S., Hayashi, S., Maruoka, S., Kumasawa, F., Mizumura, K., Jibiki, I., Matsumoto, K., Gon, Y., Kobayashi, T., et al. (2006). An inhibitory effect of A20 on NF-kappaB activation in airway epithelium upon influenza virus infection. Eur J Pharmacol 541, 198-204.
Ozawa, M., Fujii, K., Muramoto, Y., Yamada, S., Yamayoshi, S., Takada, A., Goto, H., Horimoto, T., and Kawaoka, Y. (2007). Contributions of two nuclear localization signals of influenza A virus nucleoprotein to viral replication. J Virol 81, 30-41.
Perales, B., Sanz-Ezquerro, J.J., Gastaminza, P., Ortega, J., Santaren, J.F., Ortin, J., and Nieto, A. (2000). The replication activity of influenza virus polymerase is linked to the capacity of the PA subunit to induce proteolysis. J Virol 74, 1307-1312.
Pinto, L.H., and Lamb, R.A. (2006). Influenza virus proton channels. Photochem Photobiol Sci 5, 629-632.
Pinto, L.H., and Lamb, R.A. (2007). Controlling influenza virus replication by inhibiting its proton channel. Mol Biosyst 3, 18-23.
Plotch, S.J., O''Hara, B., Morin, J., Palant, O., LaRocque, J., Bloom, J.D., Lang, S.A., Jr., DiGrandi, M.J., Bradley, M., Nilakantan, R., et al. (1999). Inhibition of influenza A virus replication by compounds interfering with the fusogenic function of the viral hemagglutinin. J Virol 73, 140-151.
Poole, E.L., Medcalf, L., Elton, D., and Digard, P. (2007). Evidence that the C-terminal PB2-binding region of the influenza A virus PB1 protein is a discrete alpha-helical domain. FEBS Lett 581, 5300-5306.
Qiu, Y., and Krug, R.M. (1994). The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A). J Virol 68, 2425-2432.
Rudneva, I.A., Kovaleva, V.P., Varich, N.L., Farashyan, V.R., Gubareva, L.V., Yamnikova, S.S., Popova, I.A., Presnova, V.P., and Kaverin, N.V. (1993). Influenza A virus reassortants with surface glycoprotein genes of the avian parent viruses: effects of HA and NA gene combinations on virus aggregation. Arch Virol 133, 437-450.
Samuel, C.E. (2001). Antiviral actions of interferons. Clin Microbiol Rev 14, 778-809, table of contents.
Si, X., Wang, Y., Wong, J., Zhang, J., McManus, B.M., and Luo, H. (2007). Dysregulation of the ubiquitin-proteasome system by curcumin suppresses coxsackievirus B3 replication. J Virol 81, 3142-3150.
Sidwell, R.W., Huffman, J.H., Khare, G.P., Allen, L.B., Witkowski, J.T., and Robins, R.K. (1972). Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide. Science 177, 705-706.
Singh, A.K., Jiang, Y., Benlhabib, E., and Gupta, S. (2007). Herbal mixtures consisting of puerarin and either polyenylphosphatidylcholine or curcumin provide comprehensive protection against alcohol-related disorders in P rats receiving free choice water and 15% ethanol in pure water. J Med Food 10, 526-542.
Singh, S., and Aggarwal, B.B. (1995). Activation of transcription factor NF-kappa B is suppressed by curcumin (diferuloylmethane) [corrected]. J Biol Chem 270, 24995-25000.
Smith, C.B., Charette, R.P., Fox, J.P., Cooney, M.K., and Hall, C.E. (1980). Lack of effect of oral ribavirin in naturally occurring influenza A virus (H1N1) infection. J Infect Dis 141, 548-554.
Song, J.M., Park, K.D., Lee, K.H., Byun, Y.H., Park, J.H., Kim, S.H., Kim, J.H., and Seong, B.L. (2007). Biological evaluation of anti-influenza viral activity of semi-synthetic catechin derivatives. Antiviral Res 76, 178-185.
Spruce, A.E., Iwata, A., White, J.M., and Almers, W. (1989). Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature 342, 555-558.
Stamatiou, G., Foscolos, G.B., Fytas, G., Kolocouris, A., Kolocouris, N., Pannecouque, C., Witvrouw, M., Padalko, E., Neyts, J., and De Clercq, E. (2003). Heterocyclic rimantadine analogues with antiviral activity. Bioorg Med Chem 11, 5485-5492.
Subbarao, K., and Joseph, T. (2007). Scientific barriers to developing vaccines against avian influenza viruses. Nat Rev Immunol 7, 267-278.
Suzuki, T., Takahashi, T., Guo, C.T., Hidari, K.I., Miyamoto, D., Goto, H., Kawaoka, Y., and Suzuki, Y. (2005). Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication. J Virol 79, 11705-11715.
Tarendeau, F., Boudet, J., Guilligay, D., Mas, P.J., Bougault, C.M., Boulo, S., Baudin, F., Ruigrok, R.W., Daigle, N., Ellenberg, J., et al. (2007). Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat Struct Mol Biol 14, 229-233.
Tsurudome, M., Gluck, R., Graf, R., Falchetto, R., Schaller, U., and Brunner, J. (1992). Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virus-induced membrane fusion. J Biol Chem 267, 20225-20232.
Turpin, E., Luke, K., Jones, J., Tumpey, T., Konan, K., and Schultz-Cherry, S. (2005). Influenza virus infection increases p53 activity: role of p53 in cell death and viral replication. J Virol 79, 8802-8811.
Urquiaga, I., and Leighton, F. (2000). Plant polyphenol antioxidants and oxidative stress. Biol Res 33, 55-64.
Vajragupta, O., Boonchoong, P., Morris, G.M., and Olson, A.J. (2005). Active site binding modes of curcumin in HIV-1 protease and integrase. Bioorg Med Chem Lett 15, 3364-3368.
von Itzstein, M., Wu, W.Y., Kok, G.B., Pegg, M.S., Dyason, J.C., Jin, B., Van Phan, T., Smythe, M.L., White, H.F., Oliver, S.W., et al. (1993). Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363, 418-423.
Wang, Y.J., Pan, M.H., Cheng, A.L., Lin, L.I., Ho, Y.S., Hsieh, C.Y., and Lin, J.K. (1997). Stability of curcumin in buffer solutions and characterization of its degradation products. J Pharm Biomed Anal 15, 1867-1876.
Wei, L., Sandbulte, M.R., Thomas, P.G., Webby, R.J., Homayouni, R., and Pfeffer, L.M. (2006). NFkappaB negatively regulates interferon-induced gene expression and anti-influenza activity. J Biol Chem 281, 11678-11684.
Wolkerstorfer, A., Kurz, H., Bachhofner, N., and Szolar, O.H. (2009). Glycyrrhizin inhibits influenza A virus uptake into the cell. Antiviral Res 83, 171-178.
Wu, W.W., Sun, Y.H., and Pante, N. (2007). Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein. Virol J 4, 49.
Zgibor, J.C., Stevenson, J.A., Rohay, J.M., Perry, S.B., Dyer, N.J., Freed, B., and Palevsky, P.M. (2003). Tracking and improving influenza immunization rates in a high-risk medicare beneficiary population. J Healthc Qual 25, 17-24, 27.
Zoidis, G., Fytas, C., Papanastasiou, I., Foscolos, G.B., Fytas, G., Padalko, E., De Clercq, E., Naesens, L., Neyts, J., and Kolocouris, N. (2006). Heterocyclic rimantadine analogues with antiviral activity. Bioorg Med Chem 14, 3341-3348.


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