Literature DB >> 2846047

Effects of fusion temperature on the lateral mobility of Sendai virus glycoproteins in erythrocyte membranes and on cell fusion indicate that glycoprotein mobilization is required for cell fusion.

B Aroeti1, Y I Henis.   

Abstract

In order to investigate the requirement for lateral mobilization of viral envelope glycoproteins on the cell surface in the induction of cell-cell fusion, we employed fluorescence photobleaching recovery to study the effect of the fusion temperature on the lateral mobilization of Sendai virus glycoproteins in the human erythrocyte membrane. As the fusion temperature was reduced below 37 degrees C (to 31 or 25 degrees C), the rates of virus-cell fusion, the accompanying hemolysis, and cell-cell fusion were all slowed down. However, the plateau (final level) after the completion of fusion was significantly reduced at lower fusion temperatures only in the case of cell-cell fusion, despite the rather similar final levels of virus-cell fusion. A concomitant decrease as a function of the fusion temperature was observed in the fraction of cell-associated viral glycoproteins that became laterally mobile in the erythrocyte membrane during fusion, and a strict correlation was found between the level of laterally mobile viral glycoproteins in the cell membrane and the final extent of cell-cell fusion. The accompanying reduction in the lateral diffusion coefficients (D) of the viral glycoproteins (1.4-fold at 31 degrees C and 1.9-fold at 25 degrees C, as compared to 37 degrees C) does not appear to determine the final level of cell-cell fusion, since fusing the cells with a higher amount of virions at 25 degrees C increased the final level of cell-cell fusion while D remained constant.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1988        PMID: 2846047     DOI: 10.1021/bi00415a039

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  7 in total

Review 1.  Membrane fusion of enveloped viruses: especially a matter of proteins.

Authors:  D Hoekstra
Journal:  J Bioenerg Biomembr       Date:  1990-04       Impact factor: 2.945

2.  Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections.

Authors:  P V Rao; T M Gallagher
Journal:  J Virol       Date:  1998-04       Impact factor: 5.103

3.  Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency virus type 1.

Authors:  S Frey; M Marsh; S Günther; A Pelchen-Matthews; P Stephens; S Ortlepp; T Stegmann
Journal:  J Virol       Date:  1995-03       Impact factor: 5.103

4.  Control of baculovirus gp64-induced syncytium formation by membrane lipid composition.

Authors:  L Chernomordik; E Leikina; M S Cho; J Zimmerberg
Journal:  J Virol       Date:  1995-05       Impact factor: 5.103

5.  Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein.

Authors:  P L Earl; B Moss; R W Doms
Journal:  J Virol       Date:  1991-04       Impact factor: 5.103

6.  A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3.

Authors:  M K Pastey; T L Gower; P W Spearman; J E Crowe; B S Graham
Journal:  Nat Med       Date:  2000-01       Impact factor: 53.440

7.  Dynamics of putative raft-associated proteins at the cell surface.

Authors:  Anne K Kenworthy; Benjamin J Nichols; Catha L Remmert; Glenn M Hendrix; Mukesh Kumar; Joshua Zimmerberg; Jennifer Lippincott-Schwartz
Journal:  J Cell Biol       Date:  2004-06-01       Impact factor: 10.539

  7 in total

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