Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein

Journal of Virology

Volumn 70, Issue 10, 1996, Pages 6653-6657

  Enami, Masayoshi ^a   Enami, Kazue ^a  

^a KANAZAWA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; VIRUS GLYCOPROTEIN; VIRUS HEMAGGLUTININ; VIRUS SIALIDASE;

ANIMAL CELL; ARTICLE; INFLUENZA VIRUS; MEMBRANE BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; VIRUS ADSORPTION; VIRUS MUTATION;

EID: 0029794377     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.10.6653-6657.1996     Document Type: Article

References (52)

1. Air, G. M., and W. G. Laver. 1989. The neuraminidase of influenza virus. Proteins 6:341-356.
2. Ausubel, F. A., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1995. Current protocols in molecular biology. Greene Publishing and Wiley-Interscience, New York.
3. Bilsel, P., M. R. Castrucci, and Y. Kawaoka. 1993. Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions. J. Virol. 67:6762-6767.
4. 2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation. Proc. Natl. Acad. Sci. USA 81:2327-2331.
5. Chong, L. D., and J. K. Rose. 1993. Membrane association of functional vesicular stomatitis virus matrix protein in vivo. J. Virol. 67:407-414.
6. Chong, L. D., and J. K. Rose. 1994. Interaction of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids. J. Virol. 68:441-447.
7. Collier, N. C., K. Knox, and M. J. Schlesinger. 1991. Inhibition of influenza virus formation by a peptide that corresponds to sequences in the cytoplasmic domain of the hemagglutinin. Virology 183:769-772.
8. Colman, P. M. 1989. Neuraminidase: enzyme and antigen, p. 175-218. In R. M. Krug (ed.), The influenza viruses. Plenum Press, New York.
9. Colman, P. M., and C. W. Ward. 1985. Structure and diversity of influenza virus neuraminidase. Curr. Top. Microbiol. Immunol. 114:178-255.
10. Davis, A. R., T. J. Bos, and D. P. Nayak. 1983. Active influenza virus neuraminidase is expressed in monkey cells from cDNA cloned in simian virus 40 vectors. Proc. Natl. Acad. Sci. USA 80:3976-3980.
11. Dubois-Dalcq, M., K. V. Holmes, and B. Rentier. 1984. Assembly of enveloped RNA viruses. Springer-Verlag, New York.
12. Enami, K., Y. Qiao, R. Fukuda, and M. Enami. 1993. An influenza virus temperature-sensitive mutant defective in the nuclear-cytoplasmic transport of the negative-sense viral RNAs. Virology 194:822-827.
13. Enami, K., T. A. Sato, S. Nakada, and M. Enami. 1994. Influenza virus NS1 protein stimulates translation of the M1 protein. J. Virol. 68:1432-1437.
14. Enami, M., W. Luytjes, M. Krystal. and P. Palese. 1990. Introduction of site-specific mutations into the genome of influenza virus. Proc. Natl. Acad. Sci. USA 87:3802-3805.
15. Enami, M., and P. Palese. 1991. High-efficiency formation of influenza virus transfectants. J. Virol. 65:2711-2713.
16. Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
17. Fujiyoshi, Y., N. P. Kume, K. Sakata, and S. B. Sato. 1994. Fine structure of influenza A virus observed by electron cryo-microscopy. EMBO J. 13:318-326.
18. Gaedigk-Nitschko, K., and M. J. Schlesinger. 1991. Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding. Virology 183:206-214.
19. García-Sastre, A., and P. Palese. 1995. The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in the packaging of this protein into viral envelopes. Virus Res. 37:37-47.
20. Hiti, A. L., and D. P. Nayak. 1982. Complete nucleotide sequence of the neuraminidase gene of human influenza virus A/WSN/33. J. Virol. 41:730-734.
21. Jin, H., G. P. Leser, and R. A. Lamb. 1995. The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity. EMBO J. 13:5504-5515.
22. Jin, H., K. Subbarao, S. Bagai, G. P. Leser, B. R. Murphy, and R. A. Lamb. 1996. Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70:1406-1414.
23. Jones, L. V., R. W. Compans, A. R. Davis, T. J. Bos, and D. P. Nayak. 1985. Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells. Mol. Cell. Biol. 5:2181-2189.
24. Kundu, A., M. A. Jabbar, and D. P. Nayak. 1991. Cell surface transport, oligomerization, and endocytosis of chimeric type II glycoprotein: role of cytoplasmic and anchor domains. Mol. Cell. Biol. 11:2675-2685.
25. Lamb, R. A. 1989. Genes and proteins of the influenza viruses, p. 1-87. In R. M. Krug (ed.), The influenza viruses. Plenum Press, New York.
26. Liu, C., and G. M. Air. 1993. Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes. Virology 194:403-407.
27. Liu, C., M. C. Eichelberger, R. W. Compans, and G. M. Air. 1995. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69:1099-1106.
28. Luytjes, W., M. Krystal, M. Enami, J. D. Parvin, and P. Palese. 1989. Amplification, expression, and packaging of a foreign gene by influenza virus. Cell 59:1107-1113.
29. Metsikkö, K., and H. Garoff. 1990. Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleo-capsid in vitro. J. Virol. 64:4678-4683.
30. Metsikkö, K., and K. Simons. 1986. The budding mechanism of spikeless vesicular stomatitis virus particles. EMBO J. 5:1913-1920.
31. Mitnaul, L. J., M. R. Castrucci, K. G. Murti, and Y. Kawaoka. 1996. The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorpolation into virions, virion morphology, and virulence in mice but is not essential for virus replication. J. Virol. 70:873-879.
32. Naim, H. Y., and M. G. Roth. 1993. Basis for selective incorporation of glycoproteins into the influenza virus envelope. J. Virol. 67:4831-4841.
33. Nayak, D. P., and M. A. Jabbar. 1989. Structural domains and organizational conformation involved in the sorting and transport of influenza virus transmembrane proteins. Annu. Rev. Microbiol. 43:465-501.
34. Nobusawa, E., T. Aoyama, H. Kato, Y. Suzuki, Y. Tateno, K. Nakajima. 1991. Comparison of complete amino acid sequences and receptor-binding properties among 13 scrotypes of hemagglutinins of influenza A viruses. Virology 182:475-485.
35. Owens, R. J., and J. K. Rose. 1993. Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus. J. Virol. 67:360-365.
36. Palese, P., K. Tobita, M. Ueda, and R. W. Compans. 1974. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397-410.
37. Pattnaik, A. K., D. J. Brown, and D. P. Nayak. 1986. Formation of influenza virus particles lacking hemagglutinin on the viral envelope. J. Virol. 60:994-1001.
38. Peeples, M. K., and M. A. Bratt. 1984. Mutation in the matrix protein of Newcastle disease virus can result in decreased fusion glycoprotein incorporation into particles and decreased infectivity. J. Virol. 51:81-90.
39. Saiki, R. K., D. H. Gelfand, S. Stoffel, S. Scharf, R. H. Higuchi, G. T. Horn, K. B. Mullis, and H. A. Erlich. 1988. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 239:487-491.
40. Sanderson, C. M., N. L. McQueen, and D. P. Nayak. 1993. Sendai virus assembly: M protein binds to viral glycoprotein in transit through the secretary pathway. J. Virol. 67:651-663.
41. Sanderson, C. M., H.-H. Wu, and D. P. Nayak. 1994. Sendai virus M protein binds independently to either the F or the HN glycoprotein in vivo. J. Virol. 68:69-76.
42. Schulman, J. L., and P. Palese. 1977. Virulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells. J. Virol. 24:170-176.
43. Shaw, M. W., R. A. Lamb, B. W. Erkkson, D. J. Briedis, and P. W. Choppin. 1982. Complete nucleotidc sequence of the neuraminidase gene of influenza B virus. Proc. Natl. Acad. Sci. USA 79:6817-6821.
44. Simpson, D. A., and R. A. Lamb. 1992. Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity. J. Virol. 66:790-803.
45. Sivasubramanian, N., and D. P. Nayak. 1987. Mutational analysis of the signal-anchor domain of influenza virus neuraminidase. Proc. Nail. Acad. Sci. USA 84:1-5.
46. Smith, G. L., J. Z. Levin, P. Palese, and B. Moss. 1987. Synthesis and cellular location of the ten influenza polypeptides individually expressed by recombinant vaccinia viruses. Virology 160:336-345.
47. Sugiura, A., M. Ueda, K. Tobita, and C. Enomoto. 1975. Further isolation and characterization of temperature-sensitive mutants of influenza virus. Virology 65:363-373.
48. Varghese, J. N., W. G. Laver, and P. M. Colman. 1983. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature (London) 305:35-40.
49. Whitt, M. A., L. Chong, and J. K. Rose. 1989. Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant. J. Virol. 63:3569-3578.
50. Yoshida, T., Y. Nagai, K. Maeno, M. Iinuma, M. Hamaguchi, T. Matsumoto, S. Nagayoshi, and M. Hoshino. 1979. Studies on the role of M protein in virus assembly using a ts mutant of HVJ (Sendai virus). Virology 92:139-154.
51. Zhao, H., B. Lindqvist, H. Garoff, C.-H. von Bonsdorff, and P. Liljestrom. 1994. A tyrosine-based motif in the cyloplasmic domain of the alphavirus envelope protein is essential for budding. EMBO J. 13:4204-4211.
52. Zurcher, T., G. Luo, and P. Palese. 1994. Mutations at palmitylation sites of the influenza virus hemanglutinin affect virus formation. J. Virol. 68:5748-5754.