Extraction of catalytically active neuraminidase of H5N1 influenza virus using thrombin proteolytic cleavage

Journal of Virological Methods

Volumn 163, Issue 1, 2010, Pages 137-143

  Wanitchang, Asawin ^a   Wongwisarnsri, Sriwan ^a   Yongkiettrakul, Suganya ^a   Jongkaewwattana, Anan ^a  

^a NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

Globular head; H5N1; Influenza A virus; Neuraminidase; Reverse genetics; Stalk; Thrombin

Indexed keywords

THROMBIN; VIRUS SIALIDASE;

AMNION FLUID; ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MODIFICATION; ENZYME RELEASE; ENZYME SUBSTRATE COMPLEX; EXTRACTION; HUMAN; HUMAN CELL; INFLUENZA VIRUS A H1N1; INFLUENZA VIRUS A H5N1; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN MOTIF; VIROGENESIS; VIRUS PARTICLE; VIRUS PURIFICATION; VIRUS RECOMBINANT;

ANIMALS; CATALYSIS; CELL LINE; CHICK EMBRYO; DOGS; HUMANS; INFLUENZA A VIRUS, H5N1 SUBTYPE; NEURAMINIDASE; PROTEIN ENGINEERING; THROMBIN;

INFLUENZA A VIRUS; ORTHOMYXOVIRIDAE;

EID: 70649104597     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2009.09.011     Document Type: Article

References (35)

1. Adamo J.E., Liu T., Schmeisser F., and Ye Z. Optimizing viral protein yield of influenza virus strain A/Vietnam/1203/2004 by modification of the neuraminidase gene. J. Virol. 83 (2009) 4023-4029
2. Air G.M., and Laver W.G. The neuraminidase of influenza virus. Proteins 6 (1989) 341-356
3. Aitken A., and Hannoun C. Purification of haemagglutinin and neuraminidase from influenza virus strain 3QB and isolation of a peptide from an antigenic region of haemagglutinin. Eur. J. Biochem. 107 (1980) 51-56
4. Cabezas J.A., Calvo P., Eid P., Martin J., Perez N., Reglero A., Rodrigo M., and Hannoun C. Studies on neuraminidase from influenza virus A(H3N2) obtained by two procedures. Int. J. Biochem. 14 (1982) 311-319
5. Castrucci M.R., and Kawaoka Y. Biologic importance of neuraminidase stalk length in influenza A virus. J. Virol. 67 (1993) 759-764
6. Chang J.Y. Thrombin specificity. Requirement for apolar amino acids adjacent to the thrombin cleavage site of polypeptide substrate. Eur. J. Biochem. 151 (1985) 217-224
7. Collins P.J., Haire L.F., Lin Y.P., Liu J., Russell R.J., Walker P.A., Skehel J.J., Martin S.R., Hay A.J., and Gamblin S.J. Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Nature 453 (2008) 1258-1261
8. Colman P.M. Influenza virus neuraminidase: structure, antibodies, and inhibitors. Protein Sci. 3 (1994) 1687-1696
9. Colman P.M., Varghese J.N., and Laver W.G. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303 (1983) 41-44
10. Crusat M., and de Jong M.D. Neuraminidase inhibitors and their role in avian and pandemic influenza. Antivir. Ther. 12 (2007) 593-602
11. Franca de Barros Jr. J., Sales Alviano D., da Silva M.H., Dutra Wigg M., Sales Alviano C., Schauer R., and dos Santos Silva Couceiro J.N. Characterization of sialidase from an influenza A (H3N2) virus strain: kinetic parameters and substrate specificity. Intervirology 46 (2003) 199-206
12. Gulati U., Wu W., Gulati S., Kumari K., Waner J.L., and Air G.M. Mismatched hemagglutinin and neuraminidase specificities in recent human H3N2 influenza viruses. Virology 339 (2005) 12-20
13. Hoffmann E., Krauss S., Perez D., Webby R., and Webster R.G. Eight-plasmid system for rapid generation of influenza virus vaccines. Vaccine 20 (2002) 3165-3170
14. Hoffmann E., Neumann G., Kawaoka Y., Hobom G., and Webster R.G. A DNA transfection system for generation of influenza A virus from eight plasmids. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 6108-6113
15. Keawcharoen J., Amonsin A., Oraveerakul K., Wattanodorn S., Papravasit T., Karnda S., Lekakul K., Pattanarangsan R., Noppornpanth S., Fouchier R.A., Osterhaus A.D., Payungporn S., Theamboonlers A., and Poovorawan Y. Characterization of the hemagglutinin and neuraminidase genes of recent influenza virus isolates from different avian species in Thailand. Acta Virol. 49 (2005) 277-280
16. Lackenby A., Thompson C.I., and Democratis J. The potential impact of neuraminidase inhibitor resistant influenza. Curr. Opin. Infect. Dis. 21 (2008) 626-638
17. Lambre C.R., Terzidis H., Greffard A., and Webster R.G. Measurement of anti-influenza neuraminidase antibody using a peroxidase-linked lectin and microtitre plates coated with natural substrates. J. Immunol. Methods 135 (1990) 49-57
18. Le Bonniec B.F., Myles T., Johnson T., Knight C.G., Tapparelli C., and Stone S.R. Characterization of the P2′ and P3′ specificities of thrombin using fluorescence-quenched substrates and mapping of the subsites by mutagenesis. Biochemistry 35 (1996) 7114-7122
19. Luo G., Chung J., and Palese P. Alterations of the stalk of the influenza virus neuraminidase: deletions and insertions. Virus Res. 29 (1993) 141-153
20. Matsuoka Y., Swayne D.E., Thomas C., Rameix-Welti M.A., Naffakh N., Warnes C., Altholtz M., Donis R., and Subbarao K. Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice. J. Virol. 83 (2009) 4704-4708
21. McKimm-Breschkin J.L., Caldwell J.B., Guthrie R.E., and Kortt A.A. A new method for the purification of the influenza A virus neuraminidase. J. Virol. Methods 32 (1991) 121-124
22. Murakami S., Horimoto T., Mai le Q., Nidom C.A., Chen H., Muramoto Y., Yamada S., Iwasa A., Iwatsuki-Horimoto K., Shimojima M., Iwata A., and Kawaoka Y. Growth determinants for H5N1 influenza vaccine seed viruses in MDCK cells. J. Virol. 82 (2008) 10502-10509
23. Ogasawara T., Gotoh B., Suzuki H., Asaka J., Shimokata K., Rott R., and Nagai Y. Expression of factor X and its significance for the determination of paramyxovirus tropism in the chick embryo. EMBO J. 11 (1992) 467-472
24. Potier M., Mameli L., Belisle M., Dallaire L., and Melancon S.B. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate. Anal. Biochem. 94 (1979) 287-296
25. Rowan A.D., Buttle D.J., and Barrett A.J. Ananain: a novel cysteine proteinase found in pineapple stem. Arch. Biochem. Biophys. 267 (1988) 262-270
26. Russell R.J., Haire L.F., Stevens D.J., Collins P.J., Lin Y.P., Blackburn G.M., Hay A.J., Gamblin S.J., and Skehel J.J. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443 (2006) 45-49
27. Sakudo A., and Ikuta K. Efficient capture of infectious H5 avian influenza virus utilizing magnetic beads coated with anionic polymer. Biochem. Biophys. Res. Commun. 377 (2008) 85-88
28. Shinya K., Hatta M., Yamada S., Takada A., Watanabe S., Halfmann P., Horimoto T., Neumann G., Kim J.H., Lim W., Guan Y., Peiris M., Kiso M., Suzuki T., Suzuki Y., and Kawaoka Y. Characterization of a human H5N1 influenza A virus isolated in 2003. J. Virol. 79 (2005) 9926-9932
29. Siniakov M.S., Kharitonenkov I.G., and Grigorjev V.B. Structure of bromelain-released influenza virus haemagglutinin as revealed by electrophoresis, sedimentation and electron microscopy. Arch. Virol. 62 (1979) 145-162
30. Trop M., and Birk Y. The specificity of proteinases from Streptomyces griseus (pronase). Biochem. J. 116 (1970) 19-25
31. Wu J.C., Peet G.W., Coutts S.J., Eckner R.J., Griffin J.A., and Farina P.R. Non-sialate inhibitor of influenza A/WSN/33 neuraminidase. Biochemistry 34 (1995) 7154-7160
32. Wu Z.L., Ethen C., Hickey G.E., and Jiang W. Active 1918 pandemic flu viral neuraminidase has distinct N-glycan profile and is resistant to trypsin digestion. Biochem. Biophys. Res. Commun. 379 (2009) 749-753
33. Yen H.L., Hoffmann E., Taylor G., Scholtissek C., Monto A.S., Webster R.G., and Govorkova E.A. Importance of neuraminidase active-site residues to the neuraminidase inhibitor resistance of influenza viruses. J. Virol. 80 (2006) 8787-8795
34. Yen H.L., Ilyushina N.A., Salomon R., Hoffmann E., Webster R.G., and Govorkova E.A. Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo. J. Virol. 81 (2007) 12418-12426
35. Yongkiettrakul S., Boonyapakron K., Jongkaewwattana A., Wanitchang A., Leartsakulpanich U., Chitnumsub P., Eurwilaichitr L., and Yuthavong Y. Avian influenza A/H5N1 neuraminidase expressed in yeast with a functional head domain. J. Virol. Methods 156 (2009) 44-51