Influence of additional acylation site(s) of influenza B virus hemagglutinin on syncytium formation

Microbiology and Immunology

Volumn 49, Issue 4, 2005, Pages 355-359

  Ujike, Makoto ^a   Nakajima, Katsuhisa ^a   Nobusawa, Eri ^a  

^a NAGOYA CITY UNIVERSITY GRADUATE SCHOOL OF MEDICAL SCIENCES   (Japan)

Author keywords

Additional acylation; Fusion; Hemagglutinin; Hydrophobicity

Indexed keywords

CYSTEINE; HEMAGGLUTININ; MEMBRANE PROTEIN;

ACYLATION; ARTICLE; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; INFLUENZA VIRUS B; NONHUMAN; POROSITY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SYNCYTIUM; VIRUS ENVELOPE; VIRUS FUSION PORE; VIRUS MORPHOLOGY; VIRUS MUTANT;

INFLUENZA B VIRUS; INFLUENZA VIRUS;

EID: 18244405312     PISSN: 03855600     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2005.tb03740.x     Document Type: Article

References (23)

1. Armstrong, R.T., Kushnir, A.S., and White, J.M. 2000. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J. Cell Biol. 151: 425-437.
2. Blumenthal, R., Sarkar, D.P., Durell, S., Howard, D.E., and Morris, S.J. 1996. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 135: 63-71.
3. Bullough, P.A., Hughson, P.M., Skehel, J.J., and Wiley, D.C. 1994. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature 371: 37-43.
4. Carr, C.M., and Kim, P.S. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73: 823-832.
5. Chernomordik, L.V., Frolov, V.A., Leikina, E., Bronk, P., and Zimmerberg, J. 1998. The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140: 1369-1382.
6. Danieli, T., Pelletier, S.L., Henis, Y.I., and White, J.M. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the conceited action of at least three hemagglutinin trimers. J. Cell Biol. 133: 559-569.
7. Fischer, C., Schroth-Diez, B., Herrmann, A., Garten, W., and Klenk, H.D. 1998. Acylation of the influenza hemagglutinin modulates fusion activity. Virology 248: 284-294.
8. Gruenke, J.A., Armstrong, R.T., Newcomb, W.W., Brown, J.C., and White, J.M. 2002. New insights into the spring-laoded conformational change of influenza virus hemagglutinin. J. Virol. 76: 4456-4466.
9. Kemble, G.W., Danieli, T., and White, J.M. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76: 383-391.
10. Kozerski, C., Ponimaskin, E., Schroth-Diez, B., Schmidt, M.F., and Herrmann, A. 2000. Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore. J. Virol. 74: 7529-7537.
11. Luo, C., Nobusawa, E., and Nakajima, K. 1999. An analysis of the role of neuraminidase in the receptor-binding activity of influenza B virus: the inhibitory effect of Zanamivir on haemadsorption. J. Gen. Virol. 80: 2969-2976.
12. Markosyan, R.M., Cohen, F.S., and Melikyan, G.B. 2000. The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores. Mol. Biol. Cell 11: 1143-1152.
13. Melikyan, G.B., Lin, S., Roth, M.G., and Cohen, F.S. 1999. Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion. Mol. Biol. Cell 10: 1821-1836.
14. Melikyan, G.B., Markosyan, R.M., Roth, M.G., and Cohen, F.S. 2000. A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion. Mol. Biol. Cell 11: 3765-3775.
15. Melikyan, G.B., White, J.M., and Cohen, F.S. 1995. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131: 679-691.
16. Naeve, C.W., and Williams, D. 1990. Patty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J. 9: 3857-3866.
17. Nobusawa, E., Aoyama, T., Kato, H., Suzuki, Y., Tateno, Y., and Nakajima, K. 1991. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182: 475-485.
18. Nobusawa, E., Hishida, R., Murata, M., Kawasaki, K., Ohnishi, S., and Nakajima, K. 1995. The role of acidic residues in the "fusion segment" of influenza A virus hemagglutinin in low-pH-dependent membrane fusion. Arch. Virol. 140: 865-875.
19. Ohuchi, M., Fischer, C., Ohuchi, R., Herwig, A., and Klenk, H.D. 1998. Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin. J. Virol. 72: 3554-3559.
20. Qiao, H., Pelletier, S.L., Hoffman, L., Hacker, J., Armstrong, R.T., and White, J.M. 1998. Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity. J. Cell Biol. 102: 1271-1283.
21. Sakai, T., Ohuchi, R., and Ohuchi, M. 2002. Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation. J. Virol. 76: 4603-4611.
22. Skehel, J.J., and Wiley, D.C. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69: 531-569.
23. Ujike, M., Nakajima, K., and Nobusawa, E. 2004. Influence of acylation sites of influenza B virus hemagglutinin on fusion pore formation and dilation. J. Virol. 78: 11536-11543.