当前位置： SCI文献检索 > JOURNAL OF VIROLOGY期刊下所有文献 > The membrane-proximal domain of vesicular stomatitis virus G protein functions as a membrane fusion potentiator and can induce hemifusion.

The membrane-proximal domain of vesicular stomatitis virus G protein functions as a membrane fusion potentiator and can induce hemifusion.

Abstract：

:Recently we showed that the membrane-proximal stem region of the vesicular stomatitis virus (VSV) G protein ectodomain (G stem [GS]), together with the transmembrane and cytoplasmic domains, was sufficient to mediate efficient VSV budding (C. S. Robison and M. A. Whitt, J. Virol. 74:2239-2246, 2000). Here, we show that GS can also potentiate the membrane fusion activity of heterologous viral fusion proteins when GS is coexpressed with those proteins. For some fusion proteins, there was as much as a 40-fold increase in syncytium formation when GS was coexpressed compared to that seen when the fusion protein was expressed alone. Fusion potentiation by GS was not protein specific, since it occurred with both pH-dependent as well as pH-independent fusion proteins. Using a recombinant vesicular stomatitis virus encoding GS that contained an N-terminal hemagglutinin (HA) tag (GS(HA) virus), we found that the GS(HA) virus bound to cells as well as the wild-type virus did at pH 7.0; however, the GS(HA) virus was noninfectious. Analysis of cells expressing GS(HA) in a three-color membrane fusion assay revealed that GS(HA) could induce lipid mixing but not cytoplasmic mixing, indicating that GS can induce hemifusion. Treatment of GS(HA) virus-bound cells with the membrane-destabilizing drug chlorpromazine rescued the hemifusion block and allowed entry and subsequent replication of GS(HA) virus, demonstrating that GS-mediated hemifusion was a functional intermediate in the membrane fusion pathway. Using a series of truncation mutants, we also determined that only 14 residues of GS, together with the VSV G transmembrane and cytoplasmic tail, were sufficient for fusion potentiation. To our knowledge, this is the first report which shows that a small domain of one viral glycoprotein can promote the fusion activity of other, unrelated viral glycoproteins.

journal_name

J Virol

journal_title

Journal of virology

authors

Jeetendra E,Robison CS,Albritton LM,Whitt MA

doi

10.1128/jvi.76.23.12300-12311.2002

subject

Has Abstract

pub_date

2002-12-01 00:00:00

pages

12300-11

issue

eissn

0022-538X

issn

1098-5514

journal_volume

pub_type

杂志文章

在线工具

The membrane-proximal domain of vesicular stomatitis virus G protein functions as a membrane fusion potentiator and can induce hemifusion.