Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
This is a preview of subscription content, log in via an institution to check access.
Tax calculation will be finalised at checkout
Purchases are for personal use only
Unable to display preview. Download preview PDF.
Allison, S. L., Schalich, J., Stiasny, K., Mandl, C. W., Kunz, C., and Heinz, F. X., 1995, Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol. 69:695–700.
Anderson, R. W. G., and Orci, L., 1988, A view of acidic intracellular compartment. J. Cell Biol. 106:539–543.
Bagai Joshi, S., Dutch, R. E., and Lamb, R. A. (1998) A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 248:20–34.
Balch, W. E., Elliott, M. M., and Keller, D. S., 1986, ATP-coupled transport of vesicular stomatitis virus G protein between the endoplasmic reticulum and the Golgi. J. Biol. Chem., 261:14681–14689.
Benmansour, A., Leblois, H., Coulon, P., Tuffereau, C., Gaudin, Y., Flamand, A., and Lafay, F., 1991, Antigenicity of rabies virus glycoprotein. J. Virol., 65:4198–4203.
Bizebard, T., Gigant, B., Rigolet, B., Rasmussen, B., Diat, O., Bosecke, P., Wharton, S.A., Skehel, J. J., and Knossow, M., 1995, Structure of influenza virus haemagglutinin complexed with a neutralizing antibody. Nature 376:92–94.
Blumenthal, R., Sarkar, D. P., Durell, S., Howard, D. E., and Morris, S. J., 1996, Dilation of the influenza hemagglutinin pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. l35:63–71.
Brunner, J., 1989, Photochemical labeling of the apolar phase of membranes. Meth. in Enzymol. 172:628–687.
Brunner, J., 1993, New photolabeling and crosslinking methods. Annual Review of Biochmistry 62:483–514.
Buckland, R., Malvoisin, E., Beauverger, P., and Wild, F., 1992, A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion. J. Gen. Virol., 73:1703–1707.
Bullough, P. A., Hughson, F. M., Skehel, J. J., add Wiley, D. C., 1994, Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37–43.
Bundo-Morita, K., Gibson, S., and Lenard, J., 1988, Radiation inactivation analysis of fusion and hemolysis by vesicular stomatitis virus Virology 163:622–424.
Carr, C. M., Chaudhry, C., and Kim, P. S., 1997, Influenza hemagglutinin is spring-loaded by a metastable native conformation. P N R SUSA 94:14306–14313.
Carr, C. M., and Kim, P. S., 1993, A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823–832.
Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S., 1997, Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263–273.
Chambers, P., Pringle, C. R., and Easton, A. J., 1990, Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins J. Gen. Virol. 71:3075–3080.
Chen, J., Ho Lee, K., Steinhauer, D. A., Stevens, D. J., Skehel, J. J., and Wiley, D. C., 1998, Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95:409–417.
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.
Chernomordik, L., Kozlov, M. M., and Zimmerberg, J., 1995, Lipids in biological membrane fusion. J. Memb. Biol. 146:1–14.
Chernomordik, L.V., Leikina, E., Frolov, V., Bronk, P., and Zimmerberg, J., 1997, An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids. J. Cell Biol. 136:81–93.
Clague, M. J., Schoch, C., Zech, L., and Blumenthal, R., 1990, Gating kinetics of pH-activated membrane fusion of vesicular stomatitis virus with cells: stopped-flow measurements by dequenching of octadecylrhodamine fluorescence. Biochemistry 29:1303–1308.
Cleverley, D. Z., and Lenard, J., 1998, The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. PN.A.S. USA 95:3425–3430.
Coulon, P, Ternaux, J. P., Flamand, A., and Tuffereau, C., 1998, An avirulent mutant of rabies virus is unable to infect motoneurons in vivo and in vitro. J. Virol. 72:273–278.
Crimmins, D. L., Mehard, W. B., and Schlesinger, S., 1983, Physical properties of a soluble form of the glycoprotein of vesicular stomatitis virus at neutral and acidic pH. Biochemistry 22:5790–5796.
Danieli, T., Pelletier, S. L., Henis, Y. I., and White, J. M., 1996, Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559–569.
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 40:431–439.
Dietzschold, B., Gore, M., Marchadier, D., Niu, H. S., Bunschoten, H. S., Otvos, L. Jr., Wunner, W. H., Ertl, H. C. J., Osterhaus, A. D. M. E., and Koprowski, H., 1990, Structural and immunological characterization of a linear neutralizing epitope of the rabies virus glycoprotein and its possible use in a synthetic vaccine. J. Virol. 64:3804–3809.
Dietzschold, B., Wiktor, T. J., Macfarlan, R., and Vanichio, A., 1982, Antigenic structure of rabies virus glycoprotein: ordering and immunological characterization of the large CNBr cleavage fragments. J. Virol. 44:595–602.
Doms, R. W., Helenius, A. H., and White, J. M., 1985, Membrane fusion activity of the influenza virus hemagglutinin: the lowpH-induced conformational change. J.Biol.Chem. 260: 2973–2981.
Doms, R. W., Keller, D. S., Helenius, A., and Balch, W., 1987, Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J. Cell Biol. 105:1957–1969.
Durell, S. R., Martin, I., Ruysschaert, J. M., Shai, Y., and Blumenthal, R., 1997, What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review). Mol. Membr. Biol. 14:97–112.
Durrer, P., Gaudin, Y., Ruigrok, R. W. H., Graf, R., and Brunner, J., 1995, Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. J. Biol. Chem. 270:17575–17581.
Fass, D., Harrison, S. C., and Kim, P. S., 1996, Retrovirus envelope domain at 1.7Å resolution. Nat. struct. Biol. 3:465–469.
Florkiewicz, R. Z., and Rose, J. K., 1984, A cell line expressing vesicular stomatitis virus glycoprotein fuses at low pH. Science 225:721–723.
Fredericksen, B. L., and Whitt, M. A., 1995, Vesicular stomatitis virus glycoprotein mutations that affect membrane fusion activity and abolish virus infectivity. J. Virol. 69:1435–1443.
Fredericksen, B. L., and Whitt, M. A., 1996, Mutations at two conserved amino acids in the glycoprotein of vesicular stomatitis virus affect pH-dependent conformational changes and reduce the pH threshold for membrane fusion. Virology 217:49–57.
Fredericksen, B. L., and Whitt, M. A., 1998, Attenuation of recombinant vesicular stomatitis viruses encoding mutant glycoproteins demonstrate a critical role for maintaining a high pH threshold for membrane fusion in viral fitness. Virology 240:349–358.
Furuta, R. A., Wild, C. T., Weng, Y., and Weiss, C. D., 1998, Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Stuct. Biol. 5:276–279.
Gastka, M. J., Horvath, J., and Lentz, T. L., 1996, Rabies virus binding to the nicotinic acetylcholine receptor a subunit demonstrated by the virus overlay protein binding assay. J. Gen. Virol. 77:2437–2440.
Gaudin, Y., 1997, Folding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperones. J. Virol. 71:3742–3750.
Gaudin, Y., De Kinkelin, P., and Benmansour, A., 1999a, Mutations in the glycoprotein of viral hemorrhagic septicemia virus that affect virulence for fish and the pH threshold for membrane fusion. J. Gen. Virol. in press.
Gaudin, Y., Moreira, S., Bénèjean, J., Blondel, D., Flamand, A., and Tuffereau, C., 1999b, Soluble ectodomain of rabies virus glycoprotein expressed in eucaryotic cells folds in a monomeric conformation which is antigenically distinct from the native state of the complete membrane-anchored glycoprotein. J. Gen. Virol. in press.
Gaudin, Y., Raux, H., Flamand, A., and Ruigrok, R. W. H., 1996, Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein. J. Virol. 70:7371–7378.
Gaudin, Y., Ruigrok, R. W. H., and Brunner, J., 1995a, Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism. J.Gen. Virol. 76:1541–1556.
Gaudin, Y., Ruigrok, R. W. H., Knossow, M., and Flamand, A., 1993, Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion. J. Virol. 67:1365–1372.
Gaudin, Y., Ruigrok, R. W. H., Tuffereau, C., Knossow, M., and Flamand, A., 1992, Rabies virus glycoprotein is a trimer. Virology 187:627–632.
Gaudin, Y., Tuffereau, C., Durrer, P., Flamand, A., and Ruigrok, R. W. H., 1995b, 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. 69:5528–5534.
Gaudin, Y., Tuffereau, C., Segretain, D., Knossow, M., and Flamand, A., 1991, Reversible conformational changes and fusion activity of rabies virus glycoprotein. J. Virol. 65:4852–4859.
Halonen, P. E., Toivanen, P., and Nikkari, T., 1974, Non-specific serum inhibitors of activity of haemagglutinins of rabies and vesicular stomatitis viruses. J. Gen. Virol. 22:309–318.
Hanson, P. I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J. E., 1997, Structure and conformational changes in NSF and its membranereceptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90:523–535.
Heinz, F. X., Stiasny, K., Püschner-Auer, G., Holzmann, H., Allison, S. L., Mandl, C. W., and Kunz, C., 1994, Structural changes and functional control of the Tick-Borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198: 109–117.
Herrmann, A., Clague, M. J., Puri, A., Morris, S. J., Blumenthal, R., and Grimaldi, S., 1990, Effect of erythrocyte transbilayer phospholipid distribution on fusion with vesicular stomatitis virus. Biochemistry 29:4054–4058.
Justman, J., Klimjack, M.R., and Kielian, M.,1993, Role of spikeprotein conformational changes in fusion of Semliki forest virus. J. Virol. 67:7597–7607.
Kemble, G. W., Danieli, T., and White, J. M., 1994, Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76:383–391.
Kenney, J. M., Sjöberg, M., Garoff, H., and Fuller, S. D., 1994, Visualization of fusion activation in the Semliki Forest virus spike. Structure 2:823–832.
Korte, T., and Herrmann, A., 1994, pH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational changeof hemagglutinin. Eur. Biophysics J. 23:105–113.
Korte, T., Ludwig, K., Krumbiegel, M., Zirwer, D., Damaschun, G., and Herrmann, A., 1997, Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy. J. Biol. Chem. 272:9764–9770.
Kraulis, P. E., 1991, MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:924–950.
Kreis, T. E., and Lodish, H. F., 1986, Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell 46:929–937.
Krumbiegel, M., Herrmann, A., and Blumenthal, R., 1994, Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin. Biophys. J. 67: 2355–2360.
Kuwert, E., Wiktor, T. J., Sokol, F., and Koprowski, H., 1968, Hemagglutination by rabies virus. J. Virol. 2:1381–1392.
Lafay, F., Benmansour, A., Chebli, K., and Flamand, A., 1996, Immunodominant epitopes defined by a yeast-expressed library of random fragments of the rabies virus glycoprotein map outside major antigenic sites. J. Gen. Virol. 77:339–346.
Lafon, M., Wiktor, T. J., and Macfarlan, R. I., 1983, Antigenic sites of the CVS rabies virus glycoprotein: analysis with monoclonal antibodies. J. Gen. Virol. 64:843–851.
Lee, J. K., and Lentz, B. R., 1998, Secretory and viral fusion may share mechanistics events with fusion between curved lipid bilayers. P.NA.S. USA 95:9274–9279.
Lentz, T. L., Burrage, T. G., Smith, A. L., Crick, J., and Tignor, G. H., 1982, Is the acetylcholine receptor a rabies receptor? Science 215:182–184.
Lentz, T. L., Wilson, P. T., Hawrot, E., and Speicher, D. W., 1984, Amino acid sequence similarity between rabies virus glycoprotein and snake venom curaremimetic neurotoxins. Science 226:2347–848.
Li, Y., Drone, C., Sat, E., and Ghosh, H. P., 1993, Mutational analysis of the vesicular stomatitis virus glycoprotein G for membrane fusion domains. J. Virol. 67:4070–4077.
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.
Lu, M., Blacklow, S. C., and Kim, P. S., 1995, A trimeric structural domain of the HIV-1 trans-membrane glycoprotein. Nat. Struct. Biol. 2:1075–1082.
Luneberg, J., Martin, I., Nussler, F., Ruysschaert, J. M., and Herrmann, A., 1995, Structure and topology of the influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:27606–27614.
Lyles, D. S., Varela, V. A., and Parce, J. W., 1990, Dynamic Nature of the quaternary structure of the vesicular stomatitis virus envelope glycoprotein. Biochemistry 29:2442–2449.
Markovic, I., Pulyaeva, H., Sokoloff, A., and Chernomordik, L. V., 1998, Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates. J. Cell Biol. 143:1155–1166.
Martin, I., Schaal, H., Scheid, A., and Ruysschaert, J. M., 1996, Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J. Virol. 70:298–304.
Mebatsion, T., König, M., and Conzelmann, K. K., 1996, Budding of rabies virus particles in the absence of the spike glycoprotein. Cell 84:941–951.
Metsikkö, K., Van Meer, G., and Simons, K., 1986, Reconstitution of the fusogenic activity of vesicular stomatitis virus. EMBO J. 5:3429–3435.
Mifune, K., Ohuchi, M., and Mannen, K., 1982, Hemolysis and cell fusion by rhabdoviruses. FEBS Lett. 137:293–297.
Nicholson, K. L., Munson, M., Miller, R. B., Filip, T. J., Fairman, R., and Hughson, F. M., 1998, Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nat. Struct. Biol. 5:793–802.
Odell, D., Wanas, E., Yan, J., and Ghosh, H. P., 1997, Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G. J. Virol. 71:7996–8000.
Ohnishi, S., 1988, Fusion of viral envelopes with cellular membranes. Curr. Top. Memb. Tramp. 32:257–296.
Pak, C. C., Puri, A., and Blumenthal, R., 1997, Conformational changes and fusion activity of vesicular stomatitis virus glycoprotein: [1251]iodonaphtyl azide photolabeling studies in biological membranes. Biochemistry 36:8890–8896.
Plonsky, I., and Zimmerberg, J., 1996, The initial fusion pore induced by baculovirus GP64 is large and forms quickly. J. Cell Biol. 135:1831–1839.
Préhaud, C., Coulon, P., Lafay, F., Thiers, C., and Flamand, A., 1988, Antigenic site II of the rabies virus glycoprotein: structure and role in viral virulence. J. Virol. 62:l-7.
Puri, A., Booy, F. P., Doms, R. W., White, J. M., and Blumenthal, R., 1990, Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatment. J. Virol 64:3824–3832.
Puri, A., Grimaldi, S., and Blumenthal, R., 1992, Role of viral envelope sialic acid in membrane fusion mediated by the vesicular stomatitis virus envelope glycoproteins. Biochemistry 31:10108–10113.
Puri, A., Winick, J., Lowry, R. J., Covell, D., Eidelman, O., Walter, A., and Blumenthal, R., 1988, Activation of vesicular stomatitis virus fusion with cells by pretreatment at low pH. J. Biol. Chem 263:4749–4753.
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. 141:1335–1347.
Ramalho-Santos, J., Nir, S., Duzgunes, N., Pato de Carvalho, A,, and Pedroso de Lima, M. C., 1993, A common mechanism for influenza virus fusion activity and inactivation. Biochemistry 32:2771–2779.
Ramsdale, E. E., Kingsman, S. M., and Kingsman, A. J., 1996, The “putative” leucine zipper region of murine leukemia virus transmembrane protein (P15e) is essential for viral infectivity. Virology 220:100–108.
Rand, R. P., 1981, Interacting phospholipid bilayers: measured forces and induced structural changes. Ann. Rev. of Biophys. Bioeng. 10:277–314.
Raux, H., Coulon, P., Lafay, F., and Flamand, A,, 1995, Monoclonal antibodies which recognize the acidic configuration of the rabies glycoprotein at the surface of the virion can be neutralizing. Virology 210:400–408.
Reitter, J. N., Sergel, T., and Morrison, T. G., 1995, Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein. J. Virol. 69:5995–6004.
Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C., and Harrison, S. C., 1995, The envelope glycoprotein from tick-borne encephalitis virus at 2Å resolution. Nature 375:291–298.
Riedel, H. C., Kondor-Koch, C., and Garoff, H., 1984, Cell surface expression of fusogenic vesicular stomatitis virus G protein from cloned cDNA. EMBO J. 3:1477–1483.
Ruigrok, R. W. H., Martin, S. R., Wharton, S. A., Skehel, J. J., Bayley, P. M., and Wiley, D. C., 1986, Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes. Virology 155:484–497.
Salminen, A., Wahlberg, J. M., Lobigs, M., Liljeström, P., and Garoff, H., 1992, Membrane fusion process of Semliki forest virus II: cleavage-dependent reorganization of the spike protein complex controls virus entry. J. Cell Biol. 116:349–457.
Sauter, N. K., Bednarski, M. D., Wurzburg, B. A., Hanson, J. E., Whitesides, G. M., Skehel, J. J., and Wiley, D. C., 1989, Hemagglutinin from two influenza virus variants bind to sialic acid derivatives with millimolar dissociations constants: a 500-Mhz proton nuclear magnetic resonance study. Biochemistry 28:8388–8396.
Schlegel, R., Tralka, M., Willingham, M. C., and Pastan, I., 1983, Inhibition of VSV binding and infectivity by phosphatidylserine: is phosphatidylserine a VSV-binding site? Cell 32:639–646.
Seif, I., Coulon, P., Rollin, P. E., and Flamand, A., 1985, Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein. J. Virol, 53:926–934.
Shokralla, S., He, Y., Wanas, E., and Ghosh, H. P., 1998, Mutations in a carboxy-terminal region of vesicular stomatitis virus glycoprotein G that affect membrane fusion activity. Virology 242:39–50.
Siegel, D. P., 1993, Energetic of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms. Biophys. J. 65:2124–2140.
Skehel, J. J., and Wiley, D. C., 1998, Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95:871–874.
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 at the pH optimum of virus-mediated membrane fusion. P.N.A.S. USA 79:968–972.
Stegmann, T., Booy, F. P., and Wilschut, J., 1987, Effects of low pH on influenza virus. J. Biol. Chem. 262:17744–17749.
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.
Stegmann, T., White, J. M., and Helenius, A., 1990, Intermediates in influenza induced membrane fusion. EMBO J. 9:4231–4241.
Stiasny, K., Allison, S. L., Marchler-Bauer, A., Kunz, C., and Heinz, F. X., 1996, Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tickborne encephalitis virus. J. Virol. 70:8142–8147.
Sugrue, R. J., Bahadur, G., Zambon, M. C., Hall-Smith, M., Douglas, A. R., and Hay, A., 1990, Specific structural alteration of the influenza hemagglutinin by amantadine. EMBO J. 9:3469–3476.
Superti, F., Derer, M., and Tsiang, H., 1984a, Mechanism of rabies virus entry into CER cells. J. Gen. Virol. 65:781–789.
Superti, E, Seganti, H., Tsiang, H., and Orci, N., 1984b, Role of phospholipids in rhabdovirus attachment to CER cells. Arch. Virol. 81:321–328.
Superti, F., Hauttecoeur, B., Morelec, M. J., Goldoni, P., Bizzini, B., and Tsiang, H., 1986, Involvement of gangliosides in rabies virus infection. J. Gen. Virol. 67:47–56.
Sutton, R. B., Fasshauer, D., Jahn, R., and Brünger, A. T., 1998, Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution. Nature 395:347–353.
Thoulouze, M. I., Lafage, M., Schachner, M., Hartmann, U., Cremer, H., and Lafon, M., 1998, The neural cell adhesion molecule is a receptor for rabies virus. J. Virol, 72:7181–7190.
Tsurudome, M., Glück, R., Graf, R., Falchetto, R., Schaller, U., and Brunner, J., 1992, Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virus-induced membrane fusion. J. Biol. Chem. 267:20225–20232
Tuffereau, C., Bénèjean, J., Blondel, D., Kieffer, B., and Flamand, A,, 1998, Low-affinity nerve-growth factor receptor (P7SNTR) can serve as a receptor for rabies virus. EMBO J. 17:7250–7259.
Tuffereau, C., Leblois, H., Bénèjean, J., Coulon, P., Lafay, F., and Flamand, A., 1989, Arginine or Lysine in position 333 of ERA and CVS glycoprotein is necessary for rabies virulence in adult mice. Virology 172:206–212.
Wahlberg, J. M., Boere, W. A. M., and Garoff, R., 1989, The heterodimeric association between the membrane proteins of Semliki forest virus changes its sensitivity to low pH during virus maturation. J. Virol. 63:4991–4997.
Wahlberg, J. M., Bron, R., Wilschut, J., and Garoff, H., 1992, Membrane fusion of Semliki forest virus involves homotrimers of the fusion protein. J. Virol. 66:7309–7318.
Wahlberg, J. M., and Garoff, H., 1992, Membrane fusion process of Semliki forest virus: low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells. J. Cell Biol. 116:339–348.
Weber, T., Paesold, G., Mischler, R., Semenza, G., and Brunner, J., 1994, Evidence for H+-induced insertion of the influenza hemagglutinin HA2 N-terminal segment into the viral membrane. J. Biol. Chem. 269:18353–18358.
Webster, R. G., Brown, L. E., and Jackson, D. C., 1983, Changes in the antigenicity of the hemagglutinin molecule of H3 influenza virus at acidic pH. Virology 126:587–599.
Weiss, W., Brown, J. H., Cusack, S., Paulson, J. C., Skehel, J. J., and Wiley, D. C., 1988, Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426–431.
Weissenhorn, W., Carfi, A., Lee, K. H., Skehel, J. J., and Wiley, D. C., 1998, Crystal structure of the Ebola virus membrane fusion subunit, Gp2, from the envelope glycoprotein ectodomain. Mol. Cell 2:605–616.
Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., and Wiley, D. C., 1997, Atomic structure of the ectodomain from HIV-1 gp41. Nature 387:426–430.
Wharton, S. A., Skehel, J. J., and Wiley, D. C., 1986, Studies of influenza haemagglutinin-mediated membrane fusion. Virology 149:27–35.
Wharton, S. A., Calder, L. J., Ruigrok, R. W. H., Skehel, J. J., Steinhauer, D. A., and Wiley, D. C., 1995, Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J. 14:240–246.
White, J., Math, K., and Helenius, A., 1981, Cell fusion by Semliki forest, Influenza and vesicular stomatitis virus. J. Cell Biol. 89:674–679.
White, J. M., Kartenbeck, J., and Helenius, A., 1982, Membrane fusion activity of influenza virus. EMBO J. 1:217–222.
White, J. M., and Wilson, I. A., 1987, Anti-peptide antibodies detect steps in a protein conformational change: low pH-activation of the influenza virus hemagglutinin. J. Cell Biol. 105:2887–2896.
Whitt, M. A., Buonocore, L., Prehaud, C., and Rose, J. K., 1991, Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 185:681–688.
Wiktor, T.J., and Koprowski, H.,1980, Antigenic variants of rabies virus. J. Exp. Med. 152:99–112.
Wilcox, M. D., McKenzie, M. O., Parce, J. W., and Lyles, D. S., 1992, Subunit interactions of vesicular stomatitis virus envelope glycoprotein influenced by detergent micelles and lipid bilayers. Biochemistry 31:10458–10464.
Wiley, D. C., and Skehel, J. J., 1987, The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Ann. Rev. Bioch. 56:365–374.
Wilson, I. A., Skehel, J. J., and Wiley, D. C., 1981, Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature 289:366–373.
Yamada, S., and Ohnishi, S., 1986, Vesicular stomatitis virus binds and fuses with phospholipid domain in target cell membranes. Biochemistry 25:3703–3708.
Yao, Y., and Compans, R. W., 1996, Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology 223: 103–112.
Yewdell, J. W., Gerhard, W., and Bächi, T., 1983, Monoclonal antihemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/8/34-mediated hemolysis. J. Virol. 48:239–248.
Zagouras, P., Ruusala, A., and Rose, J. K., 1991, Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum. J. Virol. 65:1976–1984.
Zhang, L., and Ghosh, H. P., 1994, Characterization of the putative fusogenic domain in vesicular stomatitis virus glycoprotein G. J. Virol. 68:2186–2193.
Laboratoire de Génétique des virus, CNRS, 91198, Gif sur Yvette Cedex, France
Yves Gaudin
You can also search for this author in PubMed Google Scholar
University of Antwerp, Antwerp, Belgium
Herwig Hilderson
European Molecular Biology Laboratory, Heidelberg, Germany
Stephen Fuller
© 2002 Kluwer Academic Publishers
Gaudin, Y. (2002). Reversibility in Fusion Protein Conformational Changes The Intriguing Case of Rhabdovirus-Induced Membrane Fusion. In: Hilderson, H., Fuller, S. (eds) Fusion of Biological Membranes and Related Problems. Subcellular Biochemistry, vol 34. Springer, Boston, MA. https://doi.org/10.1007/0-306-46824-7_10
DOI: https://doi.org/10.1007/0-306-46824-7_10
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-46313-6
Online ISBN: 978-0-306-46824-7
eBook Packages: Springer Book Archive
Anyone you share the following link with will be able to read this content:
Sorry, a shareable link is not currently available for this article.
Provided by the Springer Nature SharedIt content-sharing initiative