Mutations in a carboxy-terminal region of vesicular stomatitis virus glycoprotein G that affect membrane fusion activity

Virology

Volumn 242, Issue 1, 1998, Pages 39-50

  Shokralla, Shahira ^a   He, Yun ^a   Wanas, Essam ^a   Ghosh, Hara P ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; VESICULAR STOMATITIS VIRUS;

RNA VIRUSES; VESICULAR STOMATITIS VIRUS;

EID: 0032029768     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8986     Document Type: Article

References (71)

1. Anderson R. G. W., Orci L. A view of acidic intracellular compartments. J. Cell Biol. 106:1988;539-543.
2. Bhella, R., and Ghosh, H. P. Unpublished results.
3. Blacklow S. C., Lu M., Kim P. S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry. 34:1995;14955-14962.
4. Blumenthal R., Bali-Puri A., Walter A., Corell D., Eidelman O. pH dependent fusion of vesicular stomatitis virus with vero cells. J. Biol. Chem. 262:1987;13614-13619.
5. Bosch M. L., Earl P. L., Fargnoli K., Picciafuoco S., Giombini F., Wong-Staal F., Franchini G. Identification of the fusion peptide of primate immunodeficiency viruses. Science. 244:1989;694-697.
6. Brun G., Bao X. K., Prevec L. The relationship of Piry virus to other Vesiculoviruses: A re-evaluation based on the glycoprotein gene sequence. Intervirology. 38:1995;274-282.
7. Bullough P. A., Hughson F. M., Skehel J. J., Wiley D. C. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature. 371:1994;37-43.
8. Carr C. M., Kim P. S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:1993;823-832.
9. Chan D. C., Fass D., Berger J. M., Kim P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell. 89:1997;263-273.
10. Cohen C., Parry D. A. D. α-Helical coiled coils: more facts and better predictions. Science. 263:1994;488-489.
11. Coll J. M. The glycoprotein G of rhabdoviruses. Arch. Virol. 140:1995a;827-851.
12. Coll J. M. Heptad repeat sequences in the glycoprotein of rhabdoviruses. Virus Genes. 10:1995b;107-114.
13. Crimmins D., Mehard W., Schlesinger S. Physical properties of a soluble form of the glycoprotein of vesicular stomatitis virus at neutral and acidic pH. Biochemistry. 22:1983;5790-5796.
14. Crise B., Ruusala A., Zagouras P., Shaw A., Rose J. K. Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. J. Virol. 63:1989;5328-5333.
15. Daniels R. S., Downie J. C., Hay A. J., Knossow M., Skehel J. J., Wang M. L., Wiley D. C. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell. 40:1985;431-439.
16. Doms R. W., Helenius A., White J. Membrane fusion activity of the influenza virus hemagglutinin: the low pH-induced conformational change. J. Biol. Chem. 260:1985;2973-2981.
17. Doms R. W., Lamb R. A., Rose J. K., Helenius A. Folding and assembly of viral membrane proteins. Virology. 193:1993;545-562.
18. Doms R. W., Ruusala A., Machamer C., Helenius J., Helenius A., Rose J. K. Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. J. Cell Biol. 107:1988;89-99.
19. Durrer P., Gaudin Y., Ruigrok R. W., Graf R., Brunner J. Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. J. Biol. Chem. 270:1995;17575-17581.
20. Fass D., Harrison S. C., Kim P. S. Retrovirus envelope domain at 1.7Å resolution. Nature Struct. Biol. 3:1996;465-469.
21. Florkiewicz R. Z., Rose J. K. A cell line expressing vesicular stomatitis virus glycoprotein fuses at low pH. Science. 225:1984;721-723.
22. Fredericksen B. L., Whitt M. A. Vesicular stomatitis virus glycoprotein mutations that affect membrane fusion activity and abolish virus infectivity. J. Virol. 69:1995;1435-1443.
23. Fredericksen B. L., Whitt M. A. Mutations at two conserved acidic amino acids in the glycoprotein of vesicular stomatitis virus affect pH-dependent conformational changes and reduce the pH threshold for membrane fusion. Virology. 217:1996;49-57.
24. Freed E. O., Martin M. A. The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection. J. Biol. Chem. 270:1995;23883-23886.
25. Freed E. O., Myers D. J., Risser R. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl. Acad. Sci. USA. 87:1990;4650-4654.
26. Gallione C. J., Rose J. K. Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus. J. Virol. 46:1983;162-169.
27. Gaudin Y., Raux H., Flamand A., Ruigrok R. W. H. Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein. J. Virol. 70:1996;7371-7378.
28. Gaudin Y., Ruigrok R., Knossow M., Flamand A. Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion. J. Virol. 69:1993;1435-1443.
29. Gaudin Y., Ruigrok R. W. H., Brunner J. Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism. J. Gen. Virol. 76:1995a;1541-1556.
30. Gaudin Y., Tuffereau C., Durrer P., Flamand A., Ruigrok R. Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformation. J. Virol. 69:1995b;5528-5534.
31. Gething M. J., Doms R. W., York D., White J. Studies of the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:1986;11-23.
32. Guan J.-L., Machamer C. E., Rose J. K. Glycosylation allows cell surface transport of an anchored secretory protein. Cell. 42:1985;489-496.
33. Harter C., James P., Bächi T., Semenza G., Brunner W. J. J. Biol. Chem. 264:1987;6459-6464.
34. Hernandez L. D., Hoffman L. R., Wolfsberg T. G., White J. M. Virus-cell and cell-cell fusion. Annu. Rev. Cell Dev. Biol. 12:1996;627-661.
35. Horvath C. M., Lamb R. A. Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: Roles of the conserved residues in cell fusion. J. Virol. 65:1992;2443-2455.
36. Hughson F. M. Molecular mechanisms of protein-mediated membrane fusion. Curr. Opin. Struct. Biol. 5:1995;507-513.
37. Kielian M. C., Helenius A. pH induced alterations in the fusogenic spike protein of Semliki Forest virus. J. Cell Biol. 101:1985;2284-2291.
38. Koener J. F., Passavant C. W., Kurath G., Leong J. Nucleotide sequence of a cDNA clone carrying the glycoprotein gene of infectious hematopoetic necrosis virus, a fish rhabdovirus. J. Virol. 61:1987;1342-1349.
39. Kondor-Koch C., Burke B., Garoff H. Expression of Semliki Forest virus proteins from cloned complementary DNA. I. The fusion activity of the spike glycoproteins. J. Cell Biol. 97:1983;644-651.
40. Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54:1985;631-664.
41. Kreis T. E., Lodish H. F. Oligomerization is essential for transport of vesicular stomatitis virus glycoprotein to the cell surface. Cell. 46:1986;929-937.
42. Kunkel T., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-387.
43. Lamb R. W. Paromyxovirus fusion: A hypothesis for change. Virology. 197:1993;1-11.
44. Levy-Mintz P., Kielian M. Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein. J. Virol. 65:1991;4292-4300.
45. Li Y., Drone C., Sat E., Ghosh H. P. Mutational analysis of the vesicular stomatitis virus glycoprotein G for membrane fusion domains. J. Virol. 67:1993;4070-4077.
46. Lu M., Blacklow S. C., Kim P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol. 2:1995;1075-1082.
47. Lyles D., Varela V. A., Parce J. W. Dynamic nature of the quaternary structure of the VSV envelope glycoprotein. Biochemistry. 29:1990;2442-2449.
48. Masters P. S., Bhella R. S., Butcher M., Patel B., Ghosh H. P., Banerjee A. K. Structure and expression of the glycoprotein gene of Chandipura virus. Virology. 171:1989;285-290.
49. Odell D., Wanas E., Yan J., Ghosh H. P. Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G. J. Virol. 71:1997;7996-8000.
50. Ohnishi S.-I. Fusion of viral envelopes with cellular membranes. Curr. Topics Membr. Transp. 32:1988;257-298.
51. 125. Biochemistry. 36:1997;8890-8896.
52. Puri A., Winick J., Lowy J. R., Covell D., Eidelman O., Walter A., Blumenthal R. Activation of vesicular stomatitis virus fusion with cells by pretreatment at low pH. J. Biol. Chem. 263:1988;4749-4753.
53. Reidel H., Kondor-Koch C., Garoff H. Cell surface expression of fusogenic vesicular stomatitis virus G protein from cloned cDNA. EMBO J. 3:1984;1477-1483.
54. Rose J. K., Gallione C. J. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. J. Virol. 39:1981;519-528.
55. Sergel-Germans T., McQuain C., Morrison T. Mutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein that block fusion. J. Virol. 68:1994;7654-7658.
56. Skehel J. J., Bizebard T., Bullough P. A., Hughson F. M., Knossow M., Steinhauer D. A., Wharton S. A., Wiley D. C. Membrane fusion by influenza hemagglutinin. Cold Spring Harbor Symp. Quant. Biol. 60:1995;573-580.
57. Steinhauer D., Wharton S., Skehel J., Wiley D. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:1995;6643-6651.
58. 2. J. Gen. Virol. 68:1987;2625-2638.
59. Tordo N., Bourhy H., Sather S., Ollo R. Structure and expression in baculovirus of the Mokola virus glycoprotein: An efficient recombinant vaccine. Virology. 194:1993;59-69.
60. Weis W., Cusack S., Brown J., Daniels R., Skehel J., Wiley D. The structure of a membrane fusion mutant of the influenza virus hemagglutinin. EMBO J. 9:1990;17-24.
61. Weissenhorn W., Dessen A., Harrison S. C., Skehel J. J., Wiley D. C. Atomic structure of the ectodomain from HIV-1 gp41. Nature. 387:1997;426-430.
62. Wharton S. A., Ruigrok R. W. H., Martin S. R., Skehel J. J., Bayley P. M., Weis W., Wiley D. C. Conformational aspects of the acid-induced fusion mechanisms of influenza virus hemagglutinin. J. Biol. Chem. 263:1988;4474-4480.
63. White J. M. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:1990;695-697.
64. White J., Helenius A., Gething M. J. The hemagglutinin of influenza virus expressed from a cloned gene promotes membrane fusion. Nature. 300:1982;658-659.
65. White J., Maitlin K., Helenius A. Cell fusion by Semliki-Forest, influenza, and vesicular stomatitis viruses. J. Cell Biol. 89:1981;674-679.
66. Whitt M. A., Zagouras P., Crise B., Rose J. K. A fusion-defective mutant of the vesicular stomatitis virus glycoprotein. J. Virol. 64:1990;4907-4913.
67. Wiley D. C., Skehel J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:1987;365-394.
68. Yang Y.-C., Ciarletta A. B., Temple P. A., Chung M. P., Kovacic S., Witek-Giannoti J. S., Leary A. C., King R., Donahue R. E., Wong G. G., Clark S. C. Human IL-3 (Multi-CSF): Identification by expression cloning of a novel hematopoietic growth factor related to murine IL-3. Cell. 47:1986;3-10.
69. Yelverton E., Norton S., Obijeski J. F., Goeddel D. V. Rabies virus glycoprotein analogs: Biosynthesis inE.coli. Science. 219:1983;614-620.
70. Zagouras P., Ruusala A., Rose J. Dissociation and reassociation of oligomeric viral glycoportein subunits in the endoplasmic reticulum. J. Virol. 65:1991;1976-1984.
71. Zhang L., Ghosh H. P. Characterization of the putative fusogenic domain in vesicular stomatitis virus glycoprotein G. J. Virol. 68:1994;2186-2193.