Abstract
Membrane fusion and splitting play an essential role in endocytosis, transport of proteins and other materials to cellular membrane structures, and exocytosis. They also constitute an essential initial and final steps in the infection of enveloped viruses. Fusion of virus envelope with cell membranes has been most extensively studied and a wealth of informations has been accumulated (for example, White et al.,1983; Ohnishi,1987). HVJ (hemagglutinating virus of Japan) and other paramyxoviruses can fuse with cell membranes at neutral as well as acidic pH's. Other viruses, however, can fuse only at acidic pH. The different pH characteristics differentiates the cell entry mechanism for these viruses. While paramyxoviruses can transfer their genome into cytosol by fusion with cell surface membrane, the other viruses will do this by fusion in endosomes after endocytosis when the intraendosomal pH becomes lower than 6.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Bachi, T., Aguet, M.,& Howe, C.(1973). Fusion of erythrocytes by Sendai virus studied by immuno-freeze-etching. J.Virol.11, 1004–1012.
Cullis, P.R.,& Hope, M.J.(1978). Effects of fusogenic agent on membrane structure of erythrocyte ghosts and the mechanism of membrane fusion. Nature 271, 672–674.
Daniels, R.S., Downie, J.C., Hay, A.J., Knossow, M., Skehel, J.J., Wang, M.L.,& Wiley, D.C.(1985). Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40, 431–439.
Gething, M.-J., White, J.M.,& Waterfield, M.D.(1978). Purification of the fusion protein of Sendai virus: Analysis of NH2-terminal sequence generated during precursor activation. Proc.Natl.Acad.Sci.US 75, 2737–2740.
Gething, M.-J., Doms, R.W., York, D.,& White, J.(1986). Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the heamgglutinin of influenza virus. J.Cell Biol. 102, 11–23.
Hoekstra, D., de Boer, T., Klappe, K.,& Wilschut, J.(1984). Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 23,5675–5681.
Huang, R.T.C., Rott, R.,& Klenk, H.-D.(1981). Infleunza viruses cause hemolysis and fusion of cells. Virology 110, 243–247.
Kuroda, K., Kawasaki, K.,& Ohnishi, S.(1985). Kinetic analysis of fusion of hemagglutinating virus of Japan with erythrocyte membrane using spin-labeled phosphatidylcholine. Biochemistry 24, 4624–4629.
Lenard, J.,& Miller, D.K.(1981). pH-dependent hemolysis by influenza, Semliki Forest virus, and Sendai virus. Virology 110, 479–482.
Maeda, T., Asano, A., Ohki, K., Okada, Y.,& Ohnishi, S.(1975). A spin label study on fusion of red blood cells induced by hemagglutinating virus of Japan. Biochemistry 14,3736–3741.
Maeda, T.,& Ohnishi, S.(1980). Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes FEBS Lett. 122, 283–287.
Murata, M., Nagayama, K., & Ohnishi, S.(1987). Membrane Fusion Activity of Succinylated Melittin Is Triggered by Protonation of Its Carboxyl Groups. Biochemistry 26, 4056–4062.
Murata, M., Sugahara, Y., Takahasgi, S., & Ohnishi, S. pHDependent Membrane Fusion Activity of a Twenty Amino Acid Peptide of Influenza Virus Hemagglutinin. J.Biochem. 102, No.4(1987a).
Ohnishi, S.(1985). Membrane fusion: Mechanism and role in cellular response to enveloped virus, in Biomolecules Electronic Aspects (Nagata, C., Hatano, M., Tanaka, J.,& Suzuki, H.Eds), pp.227–252, Japan Scientific Societies Press, Tokyo, & Elsevier, Amsterdam.
Ohnishi, S.(1987). Membrane Fusion Activity and Mechanism of Enveloped Viruses, in Membrane Fusion in Transport, Development, and Viral Infection (Düzgünes, N., & Bronner, F. Eds), in press, Academic Press, New York.
Ruigrok, R.W.H., Wrigley, N.G., Calder, L.J., Cusack, S., Wharton, S.A., Brown, E.B.,& Skehel, J.J.(1986). Electron microscopy of low pH structure of influenza virus haemagglutinin. EMBO J. 5, 41–49.
Sato, S.B., Kawasaki, K.,& Ohnishi, S.(1983). Hemolytic activity of influenza virus hemagglutinin glycoproteins activated in mildly acidic environments. Proc.Natl.Acad.Sci.US. 80, 3153–3157.
Skehel, J.J., Bayley, P.M., Brown, E.B., Martin, S.R., Waterfield, M.D White, J.M., Wilson, I.A.,& Wiley, D.C.(1982). Changes in the conformation of infleunza virus haemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl.Acad.Sci.US. 79, 968–972.
Tsuji, A.,& Ohnishi, S,(1986). Restriction of the lateral motion of Band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state. Biochemistry 25, 6133–6139.
White, J., Kielian, M.,& Helenius, A.(1983). Membrane fusion proteins of enveloped animal viruses. Quart.Rev.Biophys. 16, 151–195.
Wilschut, J., Düzgünes, N., Fraley, R., & Papahadjopoulos, D.(1980). Studies on the mechanism of membrane fusion: Kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicle contents. Biochemistry 19, 6011–6021.
Wilson, I.A., Skehel, J.J.,& Wiley, D.C.(1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289, 366–373.
Yamada, S.,& Ohnishi, S.(1986). Vesicular stomatitis virus binds and fuses with phospholipid domain in target cell membranes. Biochemistry 25, 3703–3708.
Yoshimura, A., Yamashina, S.,& Ohnishi, S.(1985). Mobilization and aggregation of integral membrane proteins in erythro cytes induced by interaction with influenza virus at acidic pH. Exp.Cell Res. 160, 126–137.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Plenum Press, New York
About this chapter
Cite this chapter
Ohnishi, Si., Murata, M. (1988). Molecular Mechanism of Protein-Mediated Low ph-Induced Membrane Fusions. In: Ohki, S., Doyle, D., Flanagan, T.D., Hui, S.W., Mayhew, E. (eds) Molecular Mechanisms of Membrane Fusion. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1659-6_26
Download citation
DOI: https://doi.org/10.1007/978-1-4613-1659-6_26
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-8921-0
Online ISBN: 978-1-4613-1659-6
eBook Packages: Springer Book Archive