請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/34229
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 王金和(Ching-Ho Wang) | |
dc.contributor.author | Yu-Ling Cheng | en |
dc.contributor.author | 程于菱 | zh_TW |
dc.date.accessioned | 2021-06-13T05:59:03Z | - |
dc.date.available | 2016-08-10 | |
dc.date.copyright | 2011-08-10 | |
dc.date.issued | 2011 | |
dc.date.submitted | 2011-07-26 | |
dc.identifier.citation | Ada, G.L., Perry, B.T., 1954. The nucleic acid content of influenza virus. Aust. J. Exp. Biol. Med. Sci. 32(4), 453-468.
Alexander, D.J., 2000. A review of avian influenza in different bird species. Vet. Microbiol. 74(1-2), 3-13. Alexander, D.J., 2008. Orthomysovirudae-avian influenza. In: Pattison, M., McMullin, P.F., Bradbury, J.M., Alexander, D.J. (Eds.), Poultry diseases, 6th ed. Elsevier, Philadelphia, PA, pp. 317-332. Allan, G.M., McNulty, M.S., 1985. A direct immunofluorescence test for the rapid detection of avian influenza virus antigen in tissue impression smears. Avian Pathol. 14(4), 449-460. Austin, F.J., Webster, R.G., 1986. Antigenic mapping of an avian H1 influenza virus haemagglutinin and interrelationships of H1 viruses from humans, pigs and birds. J. Gen. Virol. 67 ( Pt 6), 983-992. Bahnemann, H.G., 1990. Inactivation of viral antigens for vaccine preparation with particular reference to the application of binary ethylenimine. Vaccine 8(4), 299-303. Baudin, F., Bach, C., Cusack, S., Ruigrok, R.W., 1994. Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J. 13(13), 3158-3165. Beard, C.W., Brugh, M., 1984. Laboratory Studies on the Pennsylvania Isolates of Avian Influenza (H-5 N2) in Specific Pathogen-Free Chickens. J. Am. Vet. Med. Assoc. 185(3), 340-340. Bilsel, P., Castrucci, M.R., Kawaoka, Y., 1993. Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions. J. Virol. 67(11), 6762-6767. Blaas, D., Patzelt, E., Kuechler, E., 1982. Identification of the cap binding protein of influenza virus. Nucleic Acids Res. 10(15), 4803-4812. Braam, J., Ulmanen, I., Krug, R.M., 1983. Molecular model of a eucaryotic transcription complex: functions and movements of influenza P proteins during capped RNA-primed transcription. Cell 34(2), 609-618. Brown, E.G., 2000. Influenza virus genetics. Biomed. Pharmacother. 54(4), 196-209. Bullido, R., Gomez-Puertas, P., Albo, C., Portela, A., 2000. Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein. J. Gen. Virol. 81(Pt 1), 135-142. Cappucci, D.T., Jr., Johnson, D.C., Brugh, M., Smith, T.M., Jackson, C.F., Pearson, J.E., Senne, D.A., 1985. Isolation of avian influenza virus (subtype H5N2) from chicken eggs during a natural outbreak. Avian Dis. 29(4), 1195-1200. Carrat, F., Flahault, A., 2007. Influenza vaccine: the challenge of antigenic drift. Vaccine 25(39-40), 6852-6862. Caton, A.J., Brownlee, G.G., Yewdell, J.W., Gerhard, W., 1982. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 31(2 Pt 1), 417-427. Chandler, J., Gurmin, T., Robinson, N., 2000. The place of gold in rapid tests. IVD Technology. http://www.devicelink.com/ivdt/archive/00/03/004.html. Chen, H.T., Zhang, J., Sun, D.H., Ma, L.N., Liu, X.T., Cai, X.P., Liu, Y.S., 2008. Development of reverse transcription loop-mediated isothermal amplification for rapid detection of H9 avian influenza virus. J. Virol. Methods 151(2), 200-203. Chen, W., Calvo, P.A., Malide, D., Gibbs, J., Schubert, U., Bacik, I., Basta, S., O'Neill, R., Schickli, J., Palese, P., Henklein, P., Bennink, J.R., Yewdell, J.W., 2001. A novel influenza A virus mitochondrial protein that induces cell death. Nat. Med. 7(12), 1306-1312. Cheung, T.K., Poon, L.L., 2007. Biology of influenza a virus. Ann. N. Y. Acad. Sci. 1102, 1-25. Compans, R.W., Content, J., Duesberg, P.H., 1972. Structure of the ribonucleoprotein of influenza virus. J. Virol. 10(4), 795-800. Compans, R.W., Meier-Ewert, H., Palese, P., 1974. Assembly of lipid-containing viruses. J. Supramol. Struct. 2(2-4), 496-511. Connor, R.J., Kawaoka, Y., Webster, R.G., Paulson, J.C., 1994. Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205(1), 17-23. Couceiro, J.N., Paulson, J.C., Baum, L.G., 1993. Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity. Virus Res. 29(2), 155-165. Cox, J.C., Hampson, A.W., Hamilton, R.C., 1980. An immunofluorescence study of influenza virus filament formation. Arch. Virol. 63(3-4), 275-284. Cros, J.F., Garcia-Sastre, A., Palese, P., 2005. An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein. Traffic 6(3), 205-213. Crowther, J.R., 2001. The ELISA Guidebook. Humana Press Inc., Totowa. de Boer, G.F., Back, W., Osterhaus, A.D., 1990. An ELISA for detection of antibodies against influenza A nucleoprotein in humans and various animal species. Arch. Virol. 115(1-2), 47-61. Elleman, C.J., Barclay, W.S., 2004. The M1 matrix protein controls the filamentous phenotype of influenza A virus. Virology 321(1), 144-153. Elton, D., Medcalf, L., Bishop, K., Harrison, D., Digard, P., 1999. Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding. J. Virol. 73(9), 7357-7367. Faulk, W.P., Taylor, G.M., 1971. An immunocolloid method for the electron microscope. Immunochemistry 8(11), 1081-1083. Fereidouni, S.R., Harder, T.C., Starick, E., 2008. Rapid pathotyping of recent H5N1 highly pathogenic avian influenza viruses and of H5 viruses with low pathogenicity by RT-PCR and restriction enzyme cleavage pattern (RECP). J. Virol. Methods 154(1-2), 14-19. Fouchier, R.A., Munster, V., Wallensten, A., Bestebroer, T.M., Herfst, S., Smith, D., Rimmelzwaan, G.F., Olsen, B., Osterhaus, A.D., 2005. Characterization of a novel influenza A virus hemagglutinin subtype (H16) obtained from black-headed gulls. J. Virol. 79(5), 2814-2822. Frens, G., 1973. Controlled Nucleation for the Regulation of the Particle Size in Monodisperse Gold Suspensions. Nature 241, 20-22. Frommhagen, L.H., Knight, C.A., Freeman, N.K., 1959. The ribonucleic acid, lipid, and polysaccharide constituents of influenza virus preparations. Virology 8(2), 176-197. Fujii, K., Fujii, Y., Noda, T., Muramoto, Y., Watanabe, T., Takada, A., Goto, H., Horimoto, T., Kawaoka, Y., 2005. Importance of both the coding and the segment-specific noncoding regions of the influenza A virus NS segment for its efficient incorporation into virions. J. Virol. 79(6), 3766-3774. Furuse, Y., Suzuki, A., Kamigaki, T., Oshitani, H., 2009. Evolution of the M gene of the influenza A virus in different host species: large-scale sequence analysis. Virol. J. 6, 67. Gambaryan, A., Yamnikova, S., Lvov, D., Tuzikov, A., Chinarev, A., Pazynina, G., Webster, R., Matrosovich, M., Bovin, N., 2005. Receptor specificity of influenza viruses from birds and mammals: new data on involvement of the inner fragments of the carbohydrate chain. Virology 334(2), 276-283. Garcia-Sastre, A., 2005. Interferon antagonists of influenza viruses. In: Peter, P. (Ed.), Modulation of Host Gene Expression and Innate Immunity by Viruses. Springer, Dordrecht, pp. 95-114. Geoghegan, W.D., 1988. The effect of three variables on adsorption of rabbit IgG to colloidal gold. J. Histochem. Cytochem. 36(4), 401-407. Geoghegan, W.D., Ackerman, G.A., 1977. Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: a new method, theory and application. J. Histochem. Cytochem. 25(11), 1187-1200. Glaser, L., Stevens, J., Zamarin, D., Wilson, I.A., Garcia-Sastre, A., Tumpey, T.M., Basler, C.F., Taubenberger, J.K., Palese, P., 2005. A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity. J. Virol. 79(17), 11533-11536. Gomez-Puertas, P., Albo, C., Perez-Pastrana, E., Vivo, A., Portela, A., 2000. Influenza virus matrix protein is the major driving force in virus budding. J. Virol. 74(24), 11538-11547. Gonzalez, S., Zurcher, T., Ortin, J., 1996. Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure. Nucleic Acids Res. 24(22), 4456-4463. Gorman, O.T., Bean, W.J., Kawaoka, Y., Webster, R.G., 1990. Evolution of the nucleoprotein gene of influenza A virus. J. Virol. 64(4), 1487-1497. Graves, P.N., Schulman, J.L., Young, J.F., Palese, P., 1983. Preparation of influenza virus subviral particles lacking the HA1 subunit of hemagglutinin: unmasking of cross-reactive HA2 determinants. Virology 126(1), 106-116. Guo, Y., Wang, M., Kawaoka, Y., Gorman, O., Ito, T., Saito, T., Webster, R.G., 1992. Characterization of a new avian-like influenza A virus from horses in China. Virology 188(1), 245-255. Guo, Y.R., Liu, S.Y., Gui, W.J., Zhu, G.N., 2009. Gold immunochromatographic assay for simultaneous detection of carbofuran and triazophos in water samples. Anal. Biochem. 389(1), 32-39. Hatta, M., Gao, P., Halfmann, P., Kawaoka, Y., 2001. Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293(5536), 1840-1842. Heiny, A.T., Miotto, O., Srinivasan, K.N., Khan, A.M., Zhang, G.L., Brusic, V., Tan, T.W., August, J.T., 2007. Evolutionarily conserved protein sequences of influenza a viruses, avian and human, as vaccine targets. PLoS One 2(11), e1190. Hinshaw, V.S., Bean, W.J., Geraci, J., Fiorelli, P., Early, G., Webster, R.G., 1986. Characterization of two influenza A viruses from a pilot whale. J. Virol. 58(2), 655-656. Hirst, G.K., 1941. The Agglutination of Red Cells by Allantoic Fluid of Chick Embryos Infected with Influenza Virus. Science 94(2427), 22-23. Hirst, G.K., 1942. The Quantitative Determination of Influenza Virus and Antibodies by Means of Red Cell Agglutination. J. Exp. Med. 75(1), 49-64. Huang, I.C., Li, W., Sui, J., Marasco, W., Choe, H., Farzan, M., 2008. Influenza A virus neuraminidase limits viral superinfection. J. Virol. 82(10), 4834-4843. Ito, T., Couceiro, J.N., Kelm, S., Baum, L.G., Krauss, S., Castrucci, M.R., Donatelli, I., Kida, H., Paulson, J.C., Webster, R.G., Kawaoka, Y., 1998. Molecular basis for the generation in pigs of influenza A viruses with pandemic potential. J. Virol. 72(9), 7367-7373. Jin, M., Wang, G., Zhang, R., Zhao, S., Li, H., Tan, Y., Chen, H., 2004. Development of enzyme-linked immunosorbent assay with nucleoprotein as antigen for detection of antibodies to avian influenza virus. Avian Dis. 48(4), 870-878. Kaverin, N.V., Rudneva, I.A., Ilyushina, N.A., Lipatov, A.S., Krauss, S., Webster, R.G., 2004. Structural differences among hemagglutinins of influenza A virus subtypes are reflected in their antigenic architecture: analysis of H9 escape mutants. J. Virol. 78(1), 240-249. Kaverin, N.V., Rudneva, I.A., Ilyushina, N.A., Varich, N.L., Lipatov, A.S., Smirnov, Y.A., Govorkova, E.A., Gitelman, A.K., Lvov, D.K., Webster, R.G., 2002. Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants. J. Gen. Virol. 83(Pt 10), 2497-2505. Kawaoka, Y., Chambers, T.M., Sladen, W.L., Webster, R.G., 1988. Is the gene pool of influenza viruses in shorebirds and gulls different from that in wild ducks? Virology 163(1), 247-250. Kawaoka, Y., Krauss, S., Webster, R.G., 1989. Avian-to-human transmission of the PB1 gene of influenza A viruses in the 1957 and 1968 pandemics. J. Virol. 63(11), 4603-4608. Kida, H., Ito, T., Yasuda, J., Shimizu, Y., Itakura, C., Shortridge, K.F., Kawaoka, Y., Webster, R.G., 1994. Potential for transmission of avian influenza viruses to pigs. J. Gen. Virol. 75 ( Pt 9), 2183-2188. Kim, J.A., Ryu, S.Y., Seo, S.H., 2005. Cells in the respiratory and intestinal tracts of chickens have different proportions of both human and avian influenza virus receptors. J. Microbiol. 43(4), 366-369. Kim, Y.A., Lee, E.H., Kim, K.O., Lee, Y.T., Hammock, B.D., Lee, H.S., 2011. Competitive immunochromatographic assay for the detection of the organophosphorus pesticide chlorpyrifos. Anal. Chim. Acta 693(1-2), 106-113. Kingdom, J.C.P., Kelly, T., Maclean, A.B., Mcallister, E.J., 1991. Rapid One-Step Urine Test for Human Chorionic-Gonadotropin in Evaluating Suspected Complications of Early-Pregnancy. Br. Med. J. 302(6788), 1308-1311. Kistner, O., Muller, K., Scholtissek, C., 1989. Differential phosphorylation of the nucleoprotein of influenza A viruses. J. Gen. Virol. 70 ( Pt 9), 2421-2431. Klenk, H.D., Rott, R., Orlich, M., Blodorn, J., 1975. Activation of influenza A viruses by trypsin treatment. Virology 68(2), 426-439. Klingeborn, B., Englund, L., Rott, R., Juntti, N., Rockborn, G., 1985. An avian influenza A virus killing a mammalian species--the mink. Brief report. Arch. Virol. 86(3-4), 347-351. Lahariya, C., Sharma, A.K., Pradhan, S.K., 2006. Avian flu and possible human pandemic. Indian Pediatr. 43(4), 317-325. Lang, G., Gagnon, A., Geraci, J.R., 1981. Isolation of an influenza A virus from seals. Arch. Virol. 68(3-4), 189-195. Latham, T., Galarza, J.M., 2001. Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J. Virol. 75(13), 6154-6165. Lazarowitz, S.G., Choppin, P.W., 1975. Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology 68(2), 440-454. Lee, M.S., Chang, P.C., Shien, J.H., Cheng, M.C., Shieh, H.K., 2001. Identification and subtyping of avian influenza viruses by reverse transcription-PCR. J. Virol. Methods 97(1-2), 13-22. Li, S., Schulman, J., Itamura, S., Palese, P., 1993. Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus. J. Virol. 67(11), 6667-6673. Liu, C., Eichelberger, M.C., Compans, R.W., Air, G.M., 1995. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69(2), 1099-1106. Lou, S.C., Patel, C., Ching, S., Gordon, J., 1993. One-step competitive immunochromatographic assay for semiquantitative determination of lipoprotein(a) in plasma. Clin. Chem. 39(4), 619-624. Lucocq, J.M., Roth, J., 1982. Metallic Markers for Light Microscopic Histochemistry. In: Bullock, G.R., Petrusz, P. (Eds.), Techniques in immunocytochemistry. Vol. 1. 4 vols. Academic Press, London, pp. 204-236. Mackay, I.M., Arden, K.E., Nitsche, A., 2002. Real-time PCR in virology. Nucleic Acids Res. 30(6), 1292-1305. Manzoor, R., Sakoda, Y., Sakabe, S., Mochizuki, T., Namba, Y., Tsuda, Y., Kida, H., 2008. Development of a pen-site test kit for the rapid diagnosis of H7 highly pathogenic avian influenza. J. Vet. Med. Sci. 70(6), 557-562. Martin, K., Helenius, A., 1991a. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67(1), 117-130. Martin, K., Helenius, A., 1991b. Transport of incoming influenza virus nucleocapsids into the nucleus. J. Virol. 65(1), 232-244. Matlin, K.S., Reggio, H., Helenius, A., Simons, K., 1981. Infectious entry pathway of influenza virus in a canine kidney cell line. J. Cell Biol. 91(3 Pt 1), 601-613. McGeoch, D., Fellner, P., Newton, C., 1976. Influenza virus genome consists of eight distinct RNA species. Proc. Natl. Acad. Sci. USA 73(9), 3045-3049. Meulemans, G., Carlier, M.C., Gonze, M., Petit, P., 1987. Comparison of hemagglutination-inhibition, agar gel precipitin, and enzyme-linked immunosorbent assay for measuring antibodies against influenza viruses in chickens. Avian Dis. 31(3), 560-563. Munch, M., Nielsen, L.P., Handberg, K.J., Jorgensen, P.H., 2001. Detection and subtyping (H5 and H7) of avian type A influenza virus by reverse transcription-PCR and PCR-ELISA. Arch. Virol. 146(1), 87-97. Naffakh, N., Tomoiu, A., Rameix-Welti, M.A., van der Werf, S., 2008. Host restriction of avian influenza viruses at the level of the ribonucleoproteins. Annu. Rev. Microbiol. 62, 403-424. Nath, S.T., Nayak, D.P., 1990. Function of two discrete regions is required for nuclear localization of polymerase basic protein 1 of A/WSN/33 influenza virus (H1 N1). Mol. Cell. Biol. 10(8), 4139-4145. Nayak, D.P., Hui, E.K., Barman, S., 2004. Assembly and budding of influenza virus. Virus Res. 106(2), 147-165. Neumann, G., Castrucci, M.R., Kawaoka, Y., 1997. Nuclear import and export of influenza virus nucleoprotein. J. Virol. 71(12), 9690-9700. Neumann, G., Hughes, M.T., Kawaoka, Y., 2000. Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1. EMBO J. 19(24), 6751-6758. Neumann, G., Kawaoka, Y., 2006. Host range restriction and pathogenicity in the context of influenza pandemic. Emerging Infect. Dis. 12(6), 881-886. Nieto, A., de la Luna, S., Barcena, J., Portela, A., Ortin, J., 1994. Complex structure of the nuclear translocation signal of influenza virus polymerase PA subunit. J. Gen. Virol. 75 ( Pt 1), 29-36. Noda, T., Sagara, H., Yen, A., Takada, A., Kida, H., Cheng, R.H., Kawaoka, Y., 2006. Architecture of ribonucleoprotein complexes in influenza A virus particles. Nature 439(7075), 490-492. O'Neill, R.E., Jaskunas, R., Blobel, G., Palese, P., Moroianu, J., 1995. Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J. Biol. Chem. 270(39), 22701-22704. O'Neill, R.E., Talon, J., Palese, P., 1998. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J. 17(1), 288-296. OIE, 2009a. Manual of diagnostic tests and vaccines for terrestrial animals. Chapter 2. 3. 4. Avian influenza. http://www.oie.int/international-standard-setting/ terrestrial-manual/access-online/. OIE, 2009b. Manual of diagnostic tests and vaccines for terrestrial animals. Chapter 2. 3. 14. Newcastle disease. http://www.oie.int/international-standard-setting/ terrestrial-manual/access-online/. OIE, 2010. Terrestrial Animal Health Code. Chapter 10. 4. Avian Influenza. http://www.oie.int/international-standard-setting/terrestrial-code/access-online/. OIE, 2011. Update on highly pathogenic avian influenza in animals (type H5 and H7). Avian influenza. http://www.oie.int/animal-health-in-the-world/update-on- avian-influenza/2011/. Olsen, B., Munster, V.J., Wallensten, A., Waldenstrom, J., Osterhaus, A.D., Fouchier, R.A., 2006. Global patterns of influenza a virus in wild birds. Science 312(5772), 384-388. Ortega, J., Martin-Benito, J., Zurcher, T., Valpuesta, J.M., Carrascosa, J.L., Ortin, J., 2000. Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J. Virol. 74(1), 156-163. Palese, P., Compans, R.W., 1976. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action. J. Gen. Virol. 33(1), 159-163. Palese, P., Shaw, M.L., 2007. Orthomyxoviridae: The viruses and Their replication. In: Kinipe, D.M., Howley, P.M. (Eds.), Fields' virology, 5th ed. Vol. 1. 2 vols. Lippincott Williams and Wilkins, Philadelphia, pp. 1648-1690. Palese, P., Tobita, K., Ueda, M., Compans, R.W., 1974. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61(2), 397-410. Peng, D., Hu, S., Hua, Y., Xiao, Y., Li, Z., Wang, X., Bi, D., 2007. Comparison of a new gold-immunochromatographic assay for the detection of antibodies against avian influenza virus with hemagglutination inhibition and agar gel immunodiffusion assays. Vet. Immunol. Immunopathol. 117(1-2), 17-25. Peng, F., Wang, Z., Zhang, S., Wu, R., Hu, S., Li, Z., Wang, X., Bi, D., 2008. Development of an immunochromatographic strip for rapid detection of H9 subtype avian influenza viruses. Clin. Vaccine Immunol. 15(3), 569-574. Philpott, M., Hioe, C., Sheerar, M., Hinshaw, V.S., 1990. Hemagglutinin mutations related to attenuation and altered cell tropism of a virulent avian influenza A virus. J. Virol. 64(6), 2941-2947. Pinto, L.H., Holsinger, L.J., Lamb, R.A., 1992. Influenza virus M2 protein has ion channel activity. Cell 69(3), 517-528. Poch, O., Sauvaget, I., Delarue, M., Tordo, N., 1989. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8(12), 3867-3874. Porter, A.G., Barber, C., Carey, N.H., Hallewell, R.A., Threlfall, G., Emtage, J.S., 1979. Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNA. Nature 282(5738), 471-477. Posthuma-Trumpie, G.A., Korf, J., van Amerongen, A., 2009. Lateral flow (immuno) assay: its strengths, weaknesses, opportunities and threats. A literature survey. Anal. Bioanal. Chem. 393(2), 569-582. Privalsky, M.L., Penhoet, E.E., 1981. The structure and synthesis of influenza virus phosphoproteins. J. Biol. Chem. 256(11), 5368-5376. Qian, X.Y., Alonso-Caplen, F., Krug, R.M., 1994. Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA. J. Virol. 68(4), 2433-2441. Racaniello, V.R., Palese, P., 1979. Influenza B virus genome: assignment of viral polypeptides to RNA segments. J. Virol. 29(1), 361-373. Reina, J., Fernandez-Baca, V., Blanco, I., Munar, M., 1997. Comparison of Madin-Darby canine kidney cells (MDCK) with a green monkey continuous cell line (Vero) and human lung embryonated cells (MRC-5) in the isolation of influenza A virus from nasopharyngeal aspirates by shell vial culture. J. Clin. Microbiol. 35(7), 1900-1901. Richardson, J.C., Akkina, R.K., 1991. NS2 protein of influenza virus is found in purified virus and phosphorylated in infected cells. Arch. Virol. 116(1-4), 69-80. Ritchey, M.B., Palese, P., Kilbourne, E.D., 1976. RNAs of influenza A, B, and C viruses. J. Virol. 18(2), 738-744. Rott, R., Orlich, M., Scholtissek, C., 1979. Correlation of pathogenicity and gene constellation of influenza A viruses. III. Non-pathogenic recombinants derived from highly pathogenic parent strains. J. Gen. Virol. 44(2), 471-477. Ruigrok, R.W., Calder, L.J., Wharton, S.A., 1989. Electron microscopy of the influenza virus submembranal structure. Virology 173(1), 311-316. Sanz-Ezquerro, J.J., de la Luna, S., Ortin, J., Nieto, A., 1995. Individual expression of influenza virus PA protein induces degradation of coexpressed proteins. J. Virol. 69(4), 2420-2426. Schmitt, A.P., Lamb, R.A., 2005. Influenza virus assembly and budding at the viral budozone. Adv. Virus Res. 64, 383-416. Scholtissek, C., Ludwig, S., Fitch, W.M., 1993. Analysis of influenza A virus nucleoproteins for the assessment of molecular genetic mechanisms leading to new phylogenetic virus lineages. Arch. Virol. 131(3-4), 237-250. Scholtissek, C., Rohde, W., Von Hoyningen, V., Rott, R., 1978. On the origin of the human influenza virus subtypes H2N2 and H3N2. Virology 87(1), 13-20. Schulman, J.L., Kilbourne, E.D., 1969. Independent variation in nature of hemagglutinin and neuraminidase antigens of influenza virus: distinctiveness of hemagglutinin antigen of Hong Kong-68 virus. Proc. Natl. Acad. Sci. USA 63(2), 326-333. Skehel, J.J., Bayley, P.M., Brown, E.B., Martin, S.R., Waterfield, M.D., White, J.M., Wilson, I.A., Wiley, D.C., 1982. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl. Acad. Sci. USA 79(4), 968-972. Skehel, J.J., Wiley, D.C., 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569. Sominina, A.A., Lisok, T.P., Rumel, N.B., 1977. Improved methods of influenza virus propagation. II. Characteristics of cell culture and allantoic virus preparations. Acta Virol. 21(3), 241-245. Songserm, T., Amonsin, A., Jam-on, R., Sae-Heng, N., Meemak, N., Pariyothorn, N., Payungporn, S., Theamboonlers, A., Poovorawan, Y., 2006a. Avian influenza H5N1 in naturally infected domestic cat. Emerging Infect. Dis. 12(4), 681-683. Songserm, T., Amonsin, A., Jam-on, R., Sae-Heng, N., Pariyothorn, N., Payungporn, S., Theamboonlers, A., Chutinimitkul, S., Thanawongnuwech, R., Poovorawan, Y., 2006b. Fatal avian influenza A H5N1 in a dog. Emerging Infect. Dis. 12(11), 1744-1747. Spackman, E., Senne, D.A., Myers, T.J., Bulaga, L.L., Garber, L.P., Perdue, M.L., Lohman, K., Daum, L.T., Suarez, D.L., 2002. Development of a real-time reverse transcriptase PCR assay for type A influenza virus and the avian H5 and H7 hemagglutinin subtypes. J. Clin. Microbiol. 40(9), 3256-3260. Stallknecht, D.E., Shane, S.M., 1988. Host range of avian influenza virus in free-living birds. Vet. Res. Commun. 12(2-3), 125-141. Starick, E., Romer-Oberdorfer, A., Werner, O., 2000. Type- and subtype-specific RT-PCR assays for avian influenza A viruses (AIV). J. Vet. Med. B Infect. Dis. Vet. Public Health 47(4), 295-301. Stegmann, T., 2000. Membrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion. Traffic 1(8), 598-604. Stegmann, T., Morselt, H.W., Scholma, J., Wilschut, J., 1987. Fusion of influenza virus in an intracellular acidic compartment measured by fluorescence dequenching. Biochim. Biophys. Acta 904(1), 165-170. Stieneke-Grober, A., Vey, M., Angliker, H., Shaw, E., Thomas, G., Roberts, C., Klenk, H.D., Garten, W., 1992. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11(7), 2407-2414. Suarez, D.L., Senne, D.A., Banks, J., Brown, I.H., Essen, S.C., Lee, C.W., Manvell, R.J., Mathieu-Benson, C., Moreno, V., Pedersen, J.C., Panigrahy, B., Rojas, H., Spackman, E., Alexander, D.J., 2004. Recombination resulting in virulence shift in avian influenza outbreak, Chile. Emerging Infect. Dis. 10(4), 693-699. Swayne, D.E., Halvorson, D.A., 2003. Influenza. In: Saif, Y.M., Barnes, H.J., Glisson, J.R., Fadly, A.M., MaCDougald, L.R., Swayne, D.E. (Eds.), Diseases of poultry, 11th ed. Blackwell, Ames, IA, pp. 135-160. Swayne, D.E., Senne, D.A., Beard, C.W., 1998. Avian Influenza. In: Swayne, D.E., Glisson, J.R., Jackwood, M.W., Pearson, J.E., Reed, W.M. (Eds.), A Laboratory manual for the isolation and identification of avian pathogens, 4th ed. American Association of Avian Pathologists, Kennett Square, PA, pp. 150-155. Takeuchi, K., Lamb, R.A., 1994. Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transport. J. Virol. 68(2), 911-919. Toyoda, T., Adyshev, D.M., Kobayashi, M., Iwata, A., Ishihama, A., 1996. Molecular assembly of the influenza virus RNA polymerase: determination of the subunit-subunit contact sites. J. Gen. Virol. 77 ( Pt 9), 2149-2157. Tsuchiya, E., Sugawara, K., Hongo, S., Matsuzaki, Y., Muraki, Y., Li, Z.N., Nakamura, K., 2001. Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus. J. Gen. Virol. 82(Pt 10), 2475-2484. Tsuda, Y., Sakoda, Y., Sakabe, S., Mochizuki, T., Namba, Y., Kida, H., 2007. Development of an Immunochromatographic Kit for Rapid Diagnosis of H5 Avian Influenza Virus Infection. Microbiol. Immunol. 51(9), 903-907. Twu, K.Y., Noah, D.L., Rao, P., Kuo, R.L., Krug, R.M., 2006. The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target. J. Virol. 80(8), 3957-3965. Van Deusen, R.A., Hinshaw, V.S., Senne, D.A., Pellacani, D., 1983. Micro neuraminidase-inhibition assay for classification of influenza A virus neuraminidases. Avian Dis. 27(3), 745-750. Varghese, J.N., Colman, P.M., 1991. Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. J. Mol. Biol. 221(2), 473-486. Vey, M., Orlich, M., Adler, S., Klenk, H.D., Rott, R., Garten, W., 1992. Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R. Virology 188(1), 408-413. Wang, G., Hu, S., Yu, X., 2010. Development of a latex agglutination test for detecting antibodies against avian influenza virus based on matrix 1 protein expressed in vitro. Avian Dis. 54(1), 41-45. Wang, L.C., Pan, C.H., Severinghaus, L.L., Liu, L.Y., Chen, C.T., Pu, C.E., Huang, D., Lir, J.T., Chin, S.C., Cheng, M.C., Lee, S.H., Wang, C.H., 2008. Simultaneous detection and differentiation of Newcastle disease and avian influenza viruses using oligonucleotide microarrays. Vet. Microbiol. 127(3-4), 217-226. Wang, P., Palese, P., O'Neill, R.E., 1997. The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 71(3), 1850-1856. Weber, F., Kochs, G., Gruber, S., Haller, O., 1998. A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins. Virology 250(1), 9-18. Webster, R.G., Bean, W.J., Gorman, O.T., Chambers, T.M., Kawaoka, Y., 1992. Evolution and ecology of influenza A viruses. Microbiol. Rev. 56(1), 152-179. Webster, R.G., Campbell, C.H., 1972. An inhibition test for identifying the neuraminidase antigen on influenza viruses. Avian Dis. 16(5), 1057-1066. Weis, W., Brown, J.H., Cusack, S., Paulson, J.C., Skehel, J.J., Wiley, D.C., 1988. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333(6172), 426-431. WHO, 1980. A revision of the system of nomenclature for influenza viruses: a WHO memorandum. Bull World Health Organ 58(4), 585-591. Wiley, D.C., Wilson, I.A., Skehel, J.J., 1981. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289(5796), 373-378. Wilson, I.A., Skehel, J.J., Wiley, D.C., 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289(5796), 366-373. Woolcock, P.R., Cardona, C.J., 2005. Commercial immunoassay kits for the detection of influenza virus type A: evaluation of their use with poultry. Avian Dis. 49(4), 477-481. Wright, P.F., Neumann, G., Kawaoka, Y., 2007. Orthomyxoviruses. In: Kinipe, D.M., Howley, P.M. (Eds.), Fields' virology, 5th ed. Vol. 1. 2 vols. Lippincott Williams and Wilkins, Philadelphia, pp. 1693-1741. Yamada, H., Chounan, R., Higashi, Y., Kurihara, N., Kido, H., 2004. Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria. FEBS Lett 578(3), 331-336. Yasuda, J., Nakada, S., Kato, A., Toyoda, T., Ishihama, A., 1993. Molecular assembly of influenza virus: association of the NS2 protein with virion matrix. Virology 196(1), 249-255. Zamarin, D., Ortigoza, M.B., Palese, P., 2006. Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice. J. Virol. 80(16), 7976-7983. Zhou, E.M., Chan, M., Heckert, R.A., Riva, J., Cantin, M.F., 1998. Evaluation of a competitive ELISA for detection of antibodies against avian influenza virus nucleoprotein. Avian Dis. 42(3), 517-522. Zhou, E.M., Chan, M., Heckert, R.A., Riva, J., Cantin, M.F., 2003. A Competitive Enzyme-Linked Immunosorbert Assay for Avian Influenza Serological Surveillance. Avian Dis. 47, 305-312. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/34229 | - |
dc.description.abstract | 本研究目的在於利用免疫色層分析測試片 (immunochromatographic strip;ICS) 快速檢測及簡單操作的特性,發展針對家禽流行性感冒病毒抗體之檢測方法並運用至現場。實驗中ICS主要利用固定於硝基纖維膜上的抗原,以及帶有膠體金標示的追蹤子 (tracer) 所構成。其中分別以全病毒 (A/chicken/Taiwan/2838V/00 (H6N1)) 及M1重組蛋白質 (recombinant M1;rM1) 做為抗原進行ICS之發展,並使用血球凝集抑制試驗 (hemagglutination inhibition test;HI test) 作為檢測血清之金標準 (gold standard) 進行ICS之評估。全病毒之免疫色層分析測試片 (virus-ICS) 需使用經一次冷凍解凍後之血清進行測試。使用田間血清進行測試時,其敏感性及特異性分別為95.2% (159/167) 及94.3% (150/159),但其檢測靈敏度低於HI test。至於M1重組蛋白質之免疫色層分析測試片 (rM1-ICS) 方面,rM1無法應用於rM1-ICS以進行田間陽性及陰性血清之區分。總結,本研究發展之virus-ICS仍具有應用於現場快速檢測之潛力。 | zh_TW |
dc.description.abstract | The purpose of this study was to develop immunochromatographic strips (ICS) for the detection of antibody against avian influenza virus and field application by using rapid procedure and easy operation. In our experiment, ICS was constructed by fixing antigens on the nitrocellulose membrane and the colloidal gold labeled tracer. We separately used the whole virus (A/chicken/Taiwan/2838V/00 (H6N1)) and the recombinant M1 protein (rM1) as the antigens to develop ICSs, using the hemagglutination inhibition test (HI test) as the gold standard for the evaluation of those ICSs. The virus-ICS was applied to the serum pretreated by a freeze-thaw cycle. Although the virus-ICS detection limit was lower than HI test, the sensitivity and specificity reached 95.2% (159/167) and 94.3% (150/159), respectively. On the contrary, the rM1-ICS could not be applied to distinguish the field positive and negative serum samples. In conclusion, virus-ICS could be a potential to be used as rapid test in the field. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T05:59:03Z (GMT). No. of bitstreams: 1 ntu-100-R98629010-1.pdf: 1931432 bytes, checksum: 18222e27f56fba6eee54954df3869cb3 (MD5) Previous issue date: 2011 | en |
dc.description.tableofcontents | 口試委員會審定書 i
致謝 ii 摘要 iii Abstract iv 目錄 v 表目錄 x 圖目錄 xi 第一章 序言 1 第二章 文獻回顧 3 第一節 病毒病原學 3 2-1.1 病毒分類 3 2-1.2 病毒命名 3 2-1.3 病毒結構與特徵 4 2-1.4 病毒蛋白質結構與功能 4 2-1.5 病毒複製機制 10 2-1.6 病毒變異性 11 2-1.7 病毒病原性 12 第二節 病毒流行病學 13 2-2.1 宿主範圍 13 2-2.2 病毒傳播 13 2-2.3 臨床症狀與病理變化 14 第三節 診斷方法 15 2-3.1 病毒抗原檢測 15 2-3.1.1 全病毒分離 15 2-3.1.2 血球凝集試驗 16 2-3.1.3 瓊脂膠體免疫擴散法 16 2-3.1.4 血球凝集抑制試驗 16 2-3.1.5 神經胺酸酶抑制試驗 17 2-3.1.6 偵測病毒核酸 17 2-3.1.7 偵測病毒蛋白質 18 2-3.2 病毒抗體檢測 18 2-3.2.1 瓊脂膠體免疫擴散法 18 2-3.2.2 血球凝集抑制試驗 18 2-3.2.3 神經胺酸酶抑制試驗 19 2-3.2.4 酵素聯結免疫吸附法 19 第四節 免疫色層分析測試片 19 2-4.1 免疫色層分析測試片之應用與配置 19 2-4.2 免疫色層分析測試片之標定物 20 2-4.3 免疫色層分析測試片之分類及其檢測原理 21 2-4.3.1 抗體檢測 21 2-4.3.2 抗原檢測 22 2-4.3.3 競爭型 22 第三章 材料與方法 23 第一節 血清樣本 23 3-1.1 血清樣本收集 23 3-1.2 血球凝集抑制試驗 23 3-1.3 酵素連結免疫吸附法 24 3-1.4 其他疾病之抗體檢測 24 第二節 tracer之製備與免疫色層分析測試片之組裝 25 3-2.1 抗體等電點之分析 25 3-2.2 膠體金與抗體混合比例之確定 27 3-2.3 tracer製備 27 3-2.4 免疫色層分析測試片之組裝 28 3-2.5 tracer之測試 28 第三節 發展使用全病毒之免疫色層分析測試片 (virus-ICS) 29 3-3.1 病毒製備 29 3-3.1.1 病毒增殖 29 3-3.1.2 血球凝集試驗 29 3-3.1.3 病毒核酸檢測 30 3-3.1.4 病毒濃縮 31 3-3.1.5 病毒純化 32 3-3.1.6 蛋白質定量 32 3-3.1.7 間接型ELISA 33 3-3.2 最佳化virus-ICS之條件 34 3-3.3 virus-ICS組裝及操作 34 3-3.4 virus-ICS敏感性、特異性及一致性之分析 35 3-3.5 virus-ICS檢測靈敏度之分析 36 3-3.6 virus-ICS再現性之分析 36 3-3.8 使用不同buffer稀釋血清以進行virus-ICS之測試 36 3-3.9 使用不同保存時間之血清樣本進行virus-ICS之測試 36 第四節 發展使用M1重組蛋白質之免疫色層分析測試片 (rM1-ICS) 37 3-4.1 病毒M1重組蛋白質製備 37 3-4.1.1 病毒M1基因選殖 37 3-4.1.2 重組質體之構築 39 3-4.1.3 重組質體之轉型 (transformation) 40 3-4.1.4 重組蛋白質之表現 42 3-4.1.5 重組蛋白質之純化 44 3-4.1.6 重組蛋白質之分析 45 3-4.1.7 重組蛋白質之透析 46 3-4.2 最佳化rM1-ICS之條件及血清測試 46 第四章 結果 48 第一節 血清樣本 48 第二節 tracer之製備 48 4-2.1 抗體等電點之分析 48 4-2.2 膠體金與抗體混合比例之確定 48 4-2.3 tracer之測試 49 第三節 發展使用全病毒之免疫色層分析測試片 (virus-ICS) 49 4-3.1 病毒製備 49 4-3.1.1 血球凝集試驗 49 4-3.1.2 病毒核酸檢測 49 4-3.1.3 病毒濃縮純化與蛋白質定量 49 4-3.1.4 間接型ELISA 50 4-3.2 最佳化virus-ICS之條件 50 4-3.3 virus-ICS敏感性、特異性及一致性之分析 51 4-3.4 virus-ICS檢測靈敏度之分析 51 4-3.5 virus-ICS再現性之分析 52 4-3.6 使用冷凍解凍處理前後之血清進行virus-ICS之測試 52 4-3.7 使用不同buffer稀釋血清以進行virus-ICS之測試 52 4-3.8 使用不同保存時間之血清樣本進行virus-ICS之測試 52 第四節 發展使用M1重組蛋白質之免疫色層分析測試片 (rM1-ICS) 53 4-4.1 病毒M1重組蛋白質製備 53 4-4.1.1 病毒M1基因選殖 53 4-4.1.2 重組質體之構築及轉型 53 4-4.1.3 小量重組蛋白質之表現及分析 54 4-4.1.4 重組蛋白質之表現、純化及分析 54 4-4.2 最佳化rM1-ICS之條件及血清測試 57 第五章 討論 58 第一節 使用全病毒之免疫色層分析測試片 (virus-ICS) 58 第二節 使用M1重組蛋白之免疫色層分析測試片 (rM1-ICS) 62 參考文獻 65 附錄 108 H5亞型間接型AC-ELISA 108 | |
dc.language.iso | zh-TW | |
dc.title | 家禽流行性感冒病毒抗體免疫色層分析測試片之開發 | zh_TW |
dc.title | Development of Immunochromatographic Strips for Detection of Antibody against Avian Influenza Virus | en |
dc.type | Thesis | |
dc.date.schoolyear | 99-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 謝快樂(Happy K. Shieh),沈瑞鴻(Jui-Hung Shien),陳秋麟(Chiou-Lin Chen) | |
dc.subject.keyword | 家禽流行性感冒病毒,抗體,全病毒,M1重組蛋白質,膠體金,免疫色層分析測試片, | zh_TW |
dc.subject.keyword | avian influenza virus,antibody,whole virus,recombinant M1 protein,colloidal gold,immunochromatographic strip, | en |
dc.relation.page | 114 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2011-07-26 | |
dc.contributor.author-college | 獸醫專業學院 | zh_TW |
dc.contributor.author-dept | 獸醫學研究所 | zh_TW |
顯示於系所單位: | 獸醫學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-100-1.pdf 目前未授權公開取用 | 1.89 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。