Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity

Journal of Virology

Volumn 71, Issue 5, 1997, Pages 3719-3725

  Ohuchi, Reiko ^a   Ohuchi, Masanobu ^a   Garten, Wolfgang ^a   Klenk, Hans Dieter ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM CHLORIDE; HEMAGGLUTININ; N ACETYL BETA GLUCOSAMINIDASE;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CARBOHYDRATE ANALYSIS; CELL FUSION; CONFORMATIONAL TRANSITION; ENZYME SUBUNIT; FOWL PLAGUE VIRUS; GOLGI COMPLEX; HEMADSORPTION; INFLUENZA VIRUS A; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; VIRUS MUTATION;

EID: 0030940057     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.5.3719-3725.1997     Document Type: Article

References (27)

1. Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
2. Daniels, R. S., J. C. Downie, A. J. Hey, M. Knossow, J. J. Skehel, M. C. Wang, and D. C. Wiley. 1985. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40:431-439.
3. Deshpande, K. L., V. A. Fried, M. Ando, and R. G. Webster. 1987. Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Proc. Natl. Acad. Sci. USA 84:1.
4. Fiedler, K., R. G. Parton, R. Kellner, T. Etzold, and K. Simons. 1994. VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J. 13:1729-1740.
5. Fiedler, K., and K. Simons. 1994. A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins. Cell 77:625-626.
6. Fiedler, K., and K. Simons. 1995. The role of N-glycans in the secretory pathway. Cell 81:309-312.
7. Gallagher, P. J., J. M. Henneberry, J. F. Sambrook, and M.-J. Gething. 1992. Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus. J. Virol. 66:7136-7145.
8. Hammond, C., I. Braakman, and A. Helenius. 1994. Role of N-linked oligosaccharides, glucose trimming, and calnexin during glycoprotein folding in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 91:913-917.
9. Herbert, D. N., B. Foellmer, and A. Helenius. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425-433.
10. Herbert, D. N., B. Foellmer, and A. Helenius. 1996. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglulinin in microsomes. EMBO J. 15:2961-2968.
11. Hartley, S. M., D. G. Bole, H. Hooverlitty, A. Helenius, and C. S. Copeland. 1989. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 68:426-439.
12. Kawaoka, Y., S. Yamnikova, T. M. Chambers, D. K. Lvov, and R. G. Webster. 1990. Molecular characterization of a new hemagglutinin, subtype H 14, of influenza A virus. Virology 179:759-767.
13. 1H n.m.r. and methylation analysis. EMBO J. 4:2711-2720.
14. Klenk, H.-D., and W. Garten. 1994. Activation cleavage of viral spike proteins by host proteases. In E. Wimmer (ed.), Cellular receptors for animal viruses, p. 241-280. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
15. Munk, K., E. Pritzer, E. Kretzschmar, B. Gutte, W. Garten, and H.-D. Klenk. 1992. Carbohydrate masking of an antigenic epitope of influenza virus hemagglutinin independent of oligosaccharide size. Glycobiology 2:233-240.
16. Nobusawa, E., T. Aoyama, H. Kato, Y. Suzuki, Y. Tateno, and K. Nakajima. 1991. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza viruses. Virology 182:475-485.
17. Ohuchi, M., M. Orlich, R. Ohuchi, B. E. Simpson, W. Garten, H.-D. Klenk, and R. Rott. 1989. Mutations at the cleavage site of the hemagglutinin alter the pathogenicity of influenza virus A/chick/Penn/83 (H5N2). Virology 168: 274-280.
18. Ohuchi, R., M. Ohuchi, W. Garten, and H.-D. Klenk. 1991. Human influenza virus with high sensitivity to proteolytic activation. J. Virol. 65:3530-3537.
19. Ohuchi, M., A. Cramer, M. Vey, R. Ohuchi, W. Garten, and H.-D. Klenk. 1994. Rescue of vector expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein. J. Virol. 68:920-926.
20. Ohuchi, M., A. Feldmann, R. Ohuchi, and H.-D. Klenk. 1995. Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutinating activity. Virology 212:77-83.
21. Roberts, P. C., W. Garten, and H.-D. Klenk. 1993. Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin. J. Virol. 67:3048-3060.
22. Schindler, R., C. Itin, M. Zerial, F. Lottspeich, and H.-P. Hauri. 1993. ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif. Eur. J. Cell Biol. 61:1-9.
23. Seidel, W., F. Kunkel, B. Geisler, W. Garten, B. Herrmann, L. Döhner, and H.-D. Klenk. 1991. lntraepidemic variants of influenza virus H3 hemagglutinin differing in the number of carbohydrate side chains. Arch. Virol. 120: 289-296.
24. Skehel, J. J., D. J. Stevens, R. S. Daniels, A. R. Douglas, M. Knossow, I. A. Wilson, and D. C. Wiley. 1984. A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proc. Natl. Acad. Sci. USA 81:1779-1783.
25. Takeuchi, K., and R. A. Lamb. 1994. Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transport. J. Virol. 68:911-919.
26. Vey, M., W. Schäfer, S. Berghöfer, H.-D. Klenk, and W. Garten. 1994. Maturation of the trans Golgi network protease furin: compartmentalization of zymogen activation, substrate cleavage, and C-terminal truncation. J. Cell Biol. 127:1829-1842.
27. Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-395.