R-Peptide cleavage potentiates fusion-controlling isomerization of the intersubunit disulfide in Moloney murine leukemia virus Env.

Abstract:

:Fusion of the membrane of the Moloney murine leukemia virus (Mo-MLV) Env protein is facilitated by cleavage of the R peptide from the cytoplasmic tail of its TM subunit, but the mechanism for this effect has remained obscure. The fusion is also controlled by the isomerization of the intersubunit disulfide of the Env SU-TM complex. In the present study, we used several R-peptide-cleavage-inhibited virus mutants to show that the R peptide suppresses the isomerization reaction in both in vitro and in vivo assays. Thus, the R peptide affects early steps in the activation pathway of murine leukemia virus Env.

journal_name

J Virol

journal_title

Journal of virology

authors

Löving R,Li K,Wallin M,Sjöberg M,Garoff H

doi

10.1128/JVI.02039-07

subject

Has Abstract

pub_date

2008-03-01 00:00:00

pages

2594-7

issue

5

eissn

0022-538X

issn

1098-5514

pii

JVI.02039-07

journal_volume

82

pub_type

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