Paramyxovirus Fusion: A Hypothesis for Changes

Virology

Volumn 197, Issue 1, 1993, Pages 1-11

  Lamb, Robert A ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS GLYCOPROTEIN;

HUMAN IMMUNODEFICIENCY VIRUS; INFLUENZA VIRUS; MEMBRANE FUSION; PARAMYXOVIRUS; PH; PRIORITY JOURNAL; REVIEW; VIRUS CELL INTERACTION;

AMINO ACID SEQUENCE; ANIMAL; COMPARATIVE STUDY; HIV-1; HN PROTEIN; HUMAN; INFLUENZA A VIRUS; MEMBRANE FUSION; MODELS, BIOLOGICAL; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECEPTORS, VIRUS; RESPIROVIRUS; SEMLIKI FOREST VIRUS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; VIRAL PROTEINS;

EID: 0027430672     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1006/viro.1993.1561     Document Type: Article

References (132)

1. Alkhatib, G., Richardson, C., and Shen, S. H, (1990). Intracellular processing, glycosylation, and cell-surface expression of themeasles virus fusion protein (F) encoded by a recombinant adenovirus. Virology 175, 262-270.
2. Aroeti, B.p and Henis, Y. I. (1991). Accumulation of Sendai virus glycoproteins In cell-cell contact regions and its role in cell fusion.J. Biol. Chem. 266, 15845-15849.
3. Bagai, S., Puri, A., Blumenthal, R., and Sarkar, D. P. (1993). Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Sendai virus envelopes with cells. J. Virol.67, 3312-3318.
4. Bentz, J. (Ed.) (1993), “Viral Fusion Mechanisms.” CRC Press, Boca Raton, FL.
5. Bentz, J., Ellens, H., and Alford, D. (1993). Architecture of the influenza hemagglutinin fusion site. In “Viral Fusion Mechanisms”(J. Bentz, Ed.), pp. 163-199. CRC Press, Boca Raton, FL.
6. Bosch, M. L., Earl, P. L., Fargndi, K., Picciafuoco, S., Giombini, F., Wong-Staal, F., and Franchini, G. (1989). Identifications of thefusion peptide of primate immunodeficiency viruses. Science 244, 694-696.
7. Boulay, F., Doms, R. W., Webster, R. G., and Helenius, A. (1988). Post-translational oligomerization and cooperative acid-activationof mixed influenza hemagglutinin trimers. J. Cell Biol. 106, 629-639.
8. Broeder, C. C., and Berger, E. A. (1993), CD4 molecules with a diversity of mutations encompassing the CDR3 region efficientlysupport human immunodeficiency virus type 1 envelope glycoprotein-mediated cell fusion. J. Virol. 67, 913-926.
9. Bron, R., Wahlberg, Garoff, H., and Wilschut, J. (1993). Membrane fusion of Semliki forest virus in a model system’. Correlation between fusion kinetics and structural changes in the envelopeglycoprotein. EMBO J. 12, 693-701.
10. Buckland, R., and Wild, F. (1989). Leucine zipper motif extends. Nature 338, 547.
11. Buckland, R., Malvoisin, E., Beauverger, P., and Wild, F. (1992). A leucine zipper structure present in the measles virus fusion proteinis not required for its tetramerization but is essential for fusion, JGen. Virol. 73, 1703-1707.
12. Camerini, D., and Seed, B, (1990). A CD4 domain important for HIV-mediated syncytium formation lies outside the virus binding site. Cell 60, 747-754.
13. Carr, C. M., and Kim, P. S. (1993). A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832.
14. Cattaneo, R., and Rose, J. K. (1993). Cell fusion by the envelope glycoproteins of persistent measles viruses which cause lethalhuman brain disease. J. Virol. 67, 1493-1502.
15. Chambers, P., Pringle, C. R., and Easton, A. J. (1990). Heptad repeal sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71, 3075-3080.
16. Choppin, P. W. (1964), Multiplication of a myxovirus (SV5) with minimal cytopathlc effects and without interference. Virology 23, 224-233.
17. Citovsky, V., Yanai, P., and Loyter, A. (1986). The use of circular dichroism to study conformational changes induced in Sendaivirus envelope glycoproteins. A correlation with the viral fusogenicactivity. J Biol. Chem. 261, 2235-2239.
18. Collins, P. L, and Mottet, G. (1991). Post-translational processing and oligomerization of the fusion glycoprotein of human respiratory syncytial virus. J Gen. Virol. 72, 3095-3101.
19. Daniels, R. S., Douglas, A. R., Skehel, J. J., and Wiley, D. C. (1983). Analyses of the antigenicity of influenza hemagglutinin at the pHoptimum for virus-mediated membrane fusion. J. Gen. Virol. 64, 1657-1662.
20. Daniels, R. S., Douglas, A. R.T., Skehel, J. J., Waterfield, M. D., Wilson, I. A., and Wiley, D. C. (1985a). Studies of the influenzahemagglutinin in the pH 5 conformation. In “The Origin of Pandemic Influenza Viruses" (W. G. Laver, Ed.), pp. 1-7. ElsevierJNorth-Holland, New York, NY.
21. Daniels, R. S., Downie, J. C., Hay, A. J., Knossow, M., Skehel, J. J., Wang, M. L., and Wiley, D. C. (1985). Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40, 667-675.
22. Doms, R. W., Helenius, A., and White, J. (1985), Membrane fusion activity of the influenza virus hemagglutinin. J. Biol. Chem. 260, 2973-2981.
23. Doms, R. W., and Helenius, A. (1986). Quaternary structure of influenza virus hemagglutinin after acid treatment. J. Virol. 60, 833-839.
24. Doms, R. W., Lamb, R. A., Rose, J. K., and Helenius, A. (1993). Folding and assembly of viral membrane proteins. Virology 193, 545-562.
25. Ebata, S. N., Cote, M.-J., Kang, C. Y., and Dimock, K. (1991). The fusion and hemagglutinin-neuraminidase glycoproteins of humanparainfluenza virus 3 are both required for fusion. Virology 183, 437-441.
26. Edward, J., Mann, E., and Brown, D. T. (1983). Conformational changes in Sindbis virus envelope proteins accompanying exposure to low pH. J. Virol. 45, 1090-1097.
27. Ellens, H., Bentz, J., Zheng, F., Mason, D., and White, J. (1990). The fusion site of influenza HA expressing fibroblasts requires morethan one HA trimer. Biochemistry 29, 9697-9707.
28. Ellens, H., and Larsen, C. (1993). CD4-induced change in gp120J 41 conformation and its potential relationship to fusion, in "ViralFusion Mechanisms" (J. Bentz, Ed.), pp. 291-312. CRC Press, Boca Raton, FL
29. Fields, S., Winter, G., and Brownlee, G. G. (1981). Structure of the neuraminidase in human influenza virus AJPR/8J/34. Nature 290, 213-217.
30. Fu, Y.-K., Hart, T. K., Jonak, Z. L. and Bugelski, P. J. (1993). Physio-chemical dissociation of CD4-mediated syncytium formation and shedding of human immunodeficiency virus type 1 gp120. J. Virol.67, 3818-3825.
31. Gallaher, W. R. (1987). Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus.Cell 50, 327-328.
32. Garoff, H., Frischauf, A.-M., Simons, K., Lehrach, H., and Delius, H. (1980). Nucleotide sequence of cDNA coding for Semliki forestvirus membrane glycoproteins. Nature 288, 236-241.
33. Gething, M.-J., White, J. M., and Waterfield, M. D. (1978). Purification of the fusion protein of Sendai virus: analysis of the NH2-termi-nal sequence generated during precursor activation. Proc. Natl. Acad. Sci. USA 75, 2737-2740.
34. Godley, L., Pfeifer, J., Steinhauer, D., Ely, B., Shaw, G., Kaufman, R., Suchanek, E., Pabo, C., Skehel, J. J., Wiley, D. C., and Wharton, S. (1992). Introduction of intersubunit disulfide bonds in themembrane distal region of the influenza hemagglutinin abolishesmembrane fusion activity. Cell 68, 635-645.
35. Graves, P. N., Schulman, L, Young, J. F., and Palese, P. (1983). Preparation of influenza subviral particles lacking the HA1 subunitof hemagglutinin: Unmasking of cross-reactive determinants. Virology 126, 106-116.
36. Harrison, S. C. (1986). Alphavirus structure. In “The Togaviridae and Flaviviridae” (S, Schlesinger and M. J. Schlesinger, Eds.), pp.21-57. Plenum, New York, NY.
37. Hart, T. K., Kirsh, R., Ellens, H., Sweet, R. W., Lambert, D. M., Petteway, Jr., S. R., Leary, J., and Bugelski, P. J, (1991). Binding ofsoluble CD4 proteins to human immunodeficiency virus type 1 andinfected cells induces release of envelope glycoprotein gp120.Proc. Natl. Acad. Sci. USA 88, 2189-2193.
38. Harter, C., Bachi, T., Semenza, B., and Brunner, J. (1988). Hydro-phobic photolabeling identifies BHA2 as the subunit mediating the interaction of bromelain-solubiiized influenza virus hemagglutinin with liposomes at low pH. Biochemistry 27, 1856-1864.
39. Harter, C., James, P., Bachi, T., Semenza, G., and Brunner, J. (1989). Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the “fusion peptide.” J. Biol. Chem. 264, 6459-6464.
40. Hausman, J., Kretzschmar, E., Ohuchi, M., Garten, W., and Klenk, H.-D. (1993). N1 neuraminidase of influenza virus AJFPVJRostockJ34 has hemagglutinin activity. Abstract 12th Annual MeetingAmerican Society for Virology, p A34.
41. Henis, Y. L, Herman-Barhom, B., Aroeti, B., and Gutman, O. (1989). Lateral mobility of both envelope protein (F and HN)of Sendai virusin the cell membrane is essential for cell-cell fusion. J. Biol. Chem.264, 17119-17125.
42. Heinz, F. X., Mandl, C. W., Holzmann, H., Kunz, C., Harris, B. A., Rey, F., and Harrison, S. C. (1991). The flavivirus envelope proteinE: isolation of a soluble form from tick-borne encephalitis virus andits crystallization, J. Virol. 65, 5579-5583.
43. Hiebert, S. W., Paterson, R. G., and Lamb, R. A. (1985). Hemagglutinin-neuraminidase protein of the paramyxovirus simian virus 5: Nucleotide sequence of the mRNA predicts an N-terminal membrane anchor.J. Virol. 54, 1-6.
44. Holmes, K. V., and Choppin, P. W. (1966). On the role of the response of the cell membrane in determining virus virulence: Contrasting effects of the parainfluenza virus SV5 in two cell types. J. Exp. Med. 124, 501-531.
45. Homma, M., and Ohuchi, M. (1973). Trypsin action on the growth of Sendai virus in tissue culture cells. J. Virol. 12, 1457-1465.
46. Horvath, C. M. (1992). Ph.D, dissertation. Northwestern University, Evanston, IL.
47. Horvath, C. M., and Lamb, R. A. (1992). Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of the conserved residues in cell fusion. J. Virol. 66, 2443-2455.
48. Horvath, C. M., Paterson, R. G., Shaughnessy, M. A., Wood, R., and Lamb, R. A. (1992). Biological activity of paramyxovirus fusionproteins: factors influencing formation of syncytia. J. Virol. 66, 4564-4569.
49. Hsu, M.-C., Scheid, A., and Choppin, P. W. (1979). Reconstitution of membranes with individual paramyxovirus glycoproteins and phospholipid In cholate solution. Virology 95, 476-491.
50. Hsu, M.-C., Scheid, A., and Choppin, P, W. (1981). Activation of the Sendai virus fusion protein (F) involved a conformational changewith exposure of a new hydrophobic region. J. Biol. Chem. 256, 3557-3563.
51. Hsu, M.-C., Scheid, A., and Choppin, P. W. (1982). Enhancement of membrane-fusion activity of Sendai virus by exposure of the virusto basic pH is correlated with a conformation change in the fusionprotein. Proc. Natl. Acad. Sci. USA 79, 5862-5866.
52. Hsu, M.-C., Scheid, A., and Choppin, P. W. (1983). Fusion of Sendai virus with liposomes: dependence on the viral fusion protein (F)and the lipid composition of liposomes. Virology 126, 361-369.
53. Hu, X., Ray, R., and Compans, R. W. (1992). Functional Interactions between the fusion protein and hemagglutinin-neuraminidase ofhuman parainfluenza viruses, J. Virol. 66, 1528-1534.
54. Iorio, R. M., Glickman, R. L., and Sheehan, J. P. (1992). Inhibition of fusion by neutralizing monoclonal antibodies of the hemagglutinin-neuraminidase of Newcastle disease virus. J. Gen. Virol. 73, 1167-1176.
55. Jackson, D. C., and Nestorowicz, A. (1985). Antigenic determinants of influenza virus hemagglutinin. XI. Conformational changes detected by monoclonal antibodies. Virology 145, 72-83.
56. Jain, S. K., DeCandido, S., and Kielian, M. (1991). Processing of the p62 envelope precursor protein of Semliki forest virus. J. Biol.Chem. 266, 5756-5761.
57. Kemble, G. W., Bodian, D. L., Rose, J., Wilson, I. A., and White, J. M. (1992). Intermonomer disulfide bonds impair the fusion activity ofinfluenza virus hemagglutinin. J. Virol. 66, 4940-4950.
58. Kielian, M., and Helenius, A., (1985). pH-induced alterations in the fusogenic spike protein of Semliki forest virus. J Ceil Biol. 101, 2284-2291.
59. Kielian, M. C., Marsh, M., and Helenius, A. (1986). Kinetics of endo-some acidification detected by mutant and wild-type Semliki forest virus. EMBOJ. 5, 3103-3109.
60. Kielian, M., Jungerwirth, S., Sayad, J. U., and DeCandido, S. (1990). Biosynthesis, maturation, and acid-activation of the Semliki forestvirus fusion protein, J Virol. 64, 4614-4624.
61. Klenk, H. D., Rott, R., Orlich, M., and Blodorn, J. (1975). Activation of influenza A viruses by trypsin treatment. Virology 68, 426-439.
62. Kowalski, M., Bergeron, L, Dorfman, T., Haseltine, W., and So-droski, J. (1991). Alteration of human immunodeficiency virus type 1 cytopathic effect by a mutation affecting the transmembraneenvelope glycoprotein. J. Virol. 65, 281-291.
63. Lamb, R. A. (1989). Genes and proteins of the influenza viruses, in ‘The Influenza Viruses" (R. M, Krug, Ed.), pp. 1-89. Plenum, NewYork, NY.
64. Laver, W. G., Colman, P. M., Webster, R. G., Hinshaw, V. S., and Air, G. M. (1984). Influenza virus neuraminidase with hemagglutinin activity. Virology 137, 314-323.
65. Lazarowitz, S. G., and Choppin, P. W. (1975). Enhancement of infec-tivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology 68, 440-454.
66. Levy-Mintz, P., and Kielian, M. (1991). Mutagenesis of the putative fusion domain of the Semliki forest virus spike protein. J Virol. 65, 4292-4300.
67. Lobigs, M., and Garoff, H. (1990). Fusion function of the Semliki forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62. J. Virol. 64, 1233-1240.
68. Lobigs, M., Hongxing, Z., and Garoff, H. (1990). Function of Semliki forest virus E3 peptide in virus assembly: Replacement of E3 withan artificial signal peptide abolishes spike heterodimerization andsurface expression of E1. J Virol. 64, 4346-4355.
69. Lobigs, M., Wahlberg, J. M., and Garoff, H. (1990). Spike protein oligomerization control of Semliki forest virus fusion. J Virol. 64, 5214-5218.
70. Lovejoy, B., Choe, S., Cascia, D., McRorie, D. K., DeGrado, W. F., and Eisenberg, D. (1993). Crystal structure of a synthetic triple-stranded α-helical bundle. Science 259, 1288-1293.
71. McClure, M. O., Marsh, M., and Weiss, R. A. (1988). Human immunodeficiency virus infection of CD4 bearing cells occurs by a pH independent mechanism. EMBOJ. 7, 513-518.
72. McGinnes, L. W., Semerjian, A., and Morrison, T. (1985). Conformational changes in Newcastle disease virus fusion glycoprotein during intracellular transport. J. Virol. 56, 341-348.
73. McLachian, A. D., and Stewart, M. (1975). Tropomyosin coiled-coil interactions: evidence for an unstaggered structure, J Mol. Biol.98, 293-304.
74. Merz, D. C., Scheid, A., and Choppin, P. W. (1979). Importance of antibodies to the fusion glycoprotein of paramyxoviruses in theprevention of spread of infection. J Exp. Med. 151, 275-288.
75. Miura, N., Uchida, T., and Okada, Y. (1982). HVJ (Sendai virus)-in-duced envelope fusion and cell fusion are blocked by monoclonal antl-HN protein antibody that does not inhibit hemagglutinin activity of HVJ. Exp. Cell Res. 141, 409-420.
76. Moore, J. P., McKeating, J. A., Weiss, R. A., and Sattentau, Q. J. (1990). Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250, 1139-1142.
77. Morrison, T., McQuain, C., and McGinnes, L. (1991). Complementation between avlrulent Newcastle disease virus and a fusion protein gene expressed from a retrovirus vector: requirements for membrane fusion. J. Virol. 65, 813-822.
78. Morrison, T. G., Peeples, M. E., and McGinnes, L. W. (1987). Conformational change in a viral glycoprotein during maturation due to disulfide bond disruption. Proc. Natl. Acad. Sci. USA 84, 1020-1024.
79. Morrison, T., and Fortner, A. (1991). Structure, function, and intracellular processing of the glycoproteins of paramyxoviridae. In "The Paramyxoviruses" (D. W. Kingsbury, Ed.), pp. 347-382. Plenum, New York, NY.
80. Moscona, A., and Peluso, R. W. (1991). Fusion properties of cells persistently infected with human parainfluenza virus type 3: Participation of hemagglutinin-neuraminidase in membrane fusion. J. Virol. 65, 2773-2777.
81. Moscona, A., and Peluso, R. W. (1992). Fusion properties of cells infected with human parainfluenza virus type 3: Receptor requirements for viral spread and virus-mediated membrane fusion. J.Virol. 66, 6280-6287.
82. Nakanishi, M., Uchida, T., Kim, J., and Okada, Y. (1982). Glycoproteins of Sendai virus (HVJ) have a critical ratio for fusion between virus envelopes and cell membranes. Exp. Cell Res. 142, 95-101.
83. Ng, D. T. W., Hiebert, S. W., and Lamb, R. A. (1990). Different roles of Individual N-llnked oligosaccharide chains in the folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase. Mol. Cell. Biol. 10, 1989-2001.
84. Ng, D. T. W., Watowich, S. S., and Lamb, R. A. (1992). Analysis in vivo of GRP78-BiPJsubstrate Interactions and their role in induction of the GRP78-BiP gene. Moi. Biol. Cell 3, 143-155.
85. Novick, S. L., and Hoekstra, D. (1988). Membrane penetration of Sendai virus glycoproteins during the early stage of fusion withliposomes as determined by hydrophobic photoaffinity labeling.Proc. Natl. Acad. Sci. USA 85, 7433-7437.
86. Ozawa, M., Asano, A., and Okada, Y. (1979). Biological activities of glycoproteins of HVJ (Sendai virus) studied by reconstitution ofhybrid envelope and by concanavalin A-mediated binding: A newfunction of HANA protein and structural requirement for F proteinIn hemolysis. Virology 39, 197-202.
87. Parks, G. D., and Lamb, R. A. (1990). Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains. J. Virol. 64, 3605-3616.
88. Paterson, R. G., Harris, T. J. R., and Lamb, R. A. (1984). Fusion protein of the paramyxovirus simian virus 5: Nucleotide sequenceof mRNA predicts a highly hydrophobic glycoprotein. Proc. Natl.Acad. Sci. USA 81, 6706-6710.
89. Paterson, R. G., Hiebert, S. W., and Lamb, R. A. (1985). Expression at the cel! surface of biologically active fusion and hemagglutinin-neuraminidase proteins of the paramyxovirus SV5 from clonedcDNA. Proc. Natl. Acad. Sci. USA 82, 7520-7524.
90. Paterson, R. G., and Lamb, R. A. (1987). Ability of the hydrophobic fusion related external domain of a paramyxovirus F protein to actas a membrane anchor. Cell 48, 441-452.
91. Paterson, R. G., Lvmb, R. A., Moss, B., and Murphy, B. R. (1987). Comparison of the relative roles of the F and HN surface glycoproteins of the paramyxovirus simian virus 5 in inducing protectiveImmunity. J Virol. 61, 1972-1977.
92. Paterson, R. G., Shaughnessy, M. A., and Lamb, R. A. (1989). Analysis of the relationship between cleavability of a paramyxovirus fusion protein and length of the connecting peptide. J. Virol. 63, 1293-1301.
93. Pauling, L., and Corey, R. B. (1953). Compound helical configurations of polypeptide chains: structure of protein of the α-keratin type. Nature 171, 59-61.
94. Portner, A., Scroggs, R. A., and Metzger, D. W. (1987). Distinct functions of antigenic sites of the HN glycoprotein of Sendai virus.Virology 158, 61-68.
95. Puri, A., Booy, F. P., Doms, R. W., White, J. M., and Blumenthal, R. (1990). Conformation changes and fusion activity of influenza virushemagglutinin of the H2 and H3 subtypes: Effects of acid pretreatment. J Virol. 64, 3824-3832.
96. Roos, D. S., Duchala, C. S., Stephensen, C. B., Holmes, K. V., and Choppin, P. W. (1990). Control of virus-induced cell fusion by host cell lipid composition. Virology 175, 345-357.
97. Ruigrok, R. W., Wrigley, N. G., Calder, L. J., Cusack, S., Wharton, S. A., Brown, E. B., and Skehel, J. J. (1986). Electron microscopyof the low pH structure of influenza virus haemagglutinin. EMBOJ.5, 41-49.
98. Ruigrok, R. W., Aitken, A., Calder, L. J., Martin, S. R., Skehel, J. J., Wharton, S. A., Weis, W., and Wiley, D. C. (1988). Studies on thestructure of the influenza virus haemagglutinin at the pH of membrane fusion. J. Gen. Virol. 69, 2785-2795.
99. Ruigrok, R. W. H., Hirst, E. M. A., and Hay, A. J. (1990). The specific inhibition of influenza A virus maturation by amantadine: an electron microscopic examination. J. Gen. Virol. 72, 191-194.
100. Russell, R., Paterson, R. G., and Lamb, R. A. (1993). Oligomeric structure of the paramyxovirus fusion protein, in preparation.
101. Sakai, Y., and Shibuta, H, (1989). Syncytium formation by recombinant vaccinia viruses carrying bovine parainfluenza 3 virus envelope protein genes. J. Virol. 63, 3661-3668.
102. Sato, S. B., Kawasaki, K., and Ohnishi, S. I. (1983). Hemolytic activity of influenza virus hemagglutinin glycoproteins activated in mildlyacidic environments. Proc. Natl. Acad. ScJ. USA 80, 3153-3157.
103. Sattentau, Q. J.t and Moore, J. P. (1991). Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble C04 binding. J. Exp. Med. 174, 407-415.
104. Scheid, A., Caliguiri, L. A., Compans, R. W., and Choppin, P. W. (1992). Isolation of paramyxovirus glycoproteins: Association ofboth hemagglutinating and neuraminidase activities with thelarger SV5 glycoprotein. Virology 50, 640-652.
105. Scheid, A., and Choppin, P. W. (1974a). Identification of biological activities of paramyxovirus glycoproteins: Activation of cell fusion, hemolysis, and infectivity by proteolytic cleavage of inactive precursor protein of Sendai virus. Virology 57, 475-490.
106. Scheid, A., and Choppin, P. W. (1974). The hemagglutinating and neuraminidase protein of the paramyxovirus: interaction withneuraminic acid in affinity chromatography. Virology 62, 125-133.
107. Scheid, A., and Choppin, P. W. (1977). Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virology 80, 54-66.
108. Scheid, A., Graves, M., Silver, S., and Choppin, P. W. (1978). Studies on the structure and function of paramyxovirus glycoproteins. In "Negative Strand Viruses and the Host Cell” (B. W. J. Mahy andR. D. Barry, Eds.), pp. 181-193. Academic Press, London.
109. Sechoy, O., Philippot, J. R., and Bienvenue, A, (1986). Preparation and characterization of F protein vesicles isolated from Sendaivirus by means of octyl glucoside. Biochlm. Biophys. Acta 857, 1-12.
110. Sechoy, O., Philippot, J., and Bienvenue, A. (1987). F-protein-F-pro-tein interactions with the Sendai virus identified by native bonding on chemical cross-linking. J. Biol. Chem. 262, 11519-11523.
111. Sergel, T., McGinnes, L. W., Peeples, M. E., and Morrison, T. G. (1993a). The attachment function of the Newcastle disease virushemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation. Virology 193, 717-726.
112. Sergel, T., McGinnes, L., and Morrison, T. (1993b). The HN protein of NDV has three separate activities: attachment, neuraminidase, and fusion promotion. Abstract 12th Annual Meeting AmericanSociety for Virology, p A21.
113. Skehel, J. J., Bayley, P. M., Brown, E. B., Martin, S. R., Waterfield, M. D., White, J. M., Wilson, I. A., and Wiley, D. C. (1982).Changes in the conformation of influenza virus hemagglutinin atthe pH optimum of virus-mediated membrane fusion. Proc. Natl.Acad. Sci. USA 79, 968-972.
114. Skehel, J. J., Daniels, R. S., Hay, A. J., Ruigrok, R., Wharton, S. A., Wrigley, N. G., Weiss, W., and Wiley, D. C. (1986). Structuralchanges in influenza virus haemagglutinin at the pH of membranefusion. Biochem. Soc. Trans. 14, 252-256.
115. Stegmann, T., Delfino, J. M., Richards, F. M., and Helenius, A. (1991). The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J. Biol. Chem. 266, 18404-18410.
116. Stegmann, T., White, J. M., and Helenius, A. (1991). Intermediates in influenza induced membrane fusion. EMBO J. 9, 4231-4241.
117. Stein, B. S., Gowda, S. D., Lifson, J. D., Penhallow, R. C., Beusch, K. G., and Engleman, E. G., (1987). pH independent entry into CD4positive T cells via virus envelope fusion to the plasma membrane.Cell 49, 659-668.
118. Tanabayashi, K., Takeuchi, K., Okazaki, K., Hishiyama, M., and Ya-mada, A. (1992). Expression of mumps virus glycoproteins in mammalian cells from cloned cDNAs: Both F and HN proteins arerequired for cell fusion. Virology 187, 801-804.
119. Taylor, J., Pincus, S., Tartaglia, J., Richardson, C., Alkhatib, G., Briedis, D., Appel, M., Norton, E., and Paoletti, E. (1991). Vaccinia virus recombinants expressing either the measles virus fusion or hemagglutinin glycoprotein protect dogs against caninedistemper virus challenge. J Virol. 65, 4263-4274.
120. Tsurooome, M., Hamada, A., Hishiyama, M., and Ito, Y. (1986). Monoclonal antibodies against the glycoproteins of mumps virus:fusion inhibition by anti-HN monoclonal antibody. J Gen. Virol. 67, 2259-2265.
121. Wahlberg, J. M., and Garoff, H. (1992). Membrane fusion process of Semliki forest virus I: Low pH induced rearrangement in spikeprotein quarternary structure precedes virus penetration into cells.J Cell Biol. 116, 339-348.
122. Wahlberg, J. M., Bron, R., Wilschut, J., and Garoff, H. (1992). Membrane fusion of Semliki forest virus involves homotrlmers ofthe fusion protein, J. Virol. 66, 7309-7318.
123. Webster, R. G., Brown, L. E., and Jackson, D, C. (1983). Changes in the antigenicity of the hemagglutinin molecules of H3 influenzavirus at acidic pH, Virology 126, 587-599.
124. White, J., Matlin, K., and Helenius, A. (1981). Cel! fusion by Semliki forest, influenza and vesicular stomatitis viruses. J. Cell Biol. 89, 674-679.
125. White, J., and Wilson, I. A. (1987). Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation ofthe influenza virus hemagglutinin. J Ceil Biol. 105, 2887-2896.
126. White, J. M. (1990). Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52, 675-697.
127. White, J. M. (1992). Membrane fusion. Science 258, 917-924.
128. Wild, T. F., Malvoisin, E., and Buckland, R. (1991). Measles virus: Both the hemagglutinin and fusion glycoproteins are required forfusion, J. Gen. Virol. 72, 439-442.
129. Wiley, D. C., and Skehel, J. J. (1987). The structure and function of the hemagglutinin membrane glycoprotein of Influenza virus.Annu. Rev. Biochem. 56, 365-394.
130. Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Aresolution. Nature 289, 366-375.
131. Wong-Staal, F. (1990). Human immunodeficiency viruses and their replication. In "Fields’ Virology” (B. N. Fields and D. M. Knipe, Eds.), pp. 1529-1543. Raven Press, New York, NY.
132. Yewdell, J. W., Gerhard, W., and Bachi, T. (1983). Monoclonal antihemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus AJPRJ8J34-mediated hemolysis. J. Virol. 48, 239-248.