Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein.

Abstract:

:The alphavirus Semliki Forest virus (SFV) infects cells through low-pH-induced membrane fusion mediated by the E1 protein, a class II virus membrane fusion protein. During fusion, E1 inserts into target membranes via its hydrophobic fusion loop and refolds to form a stable E1 homotrimer. Mutation of a highly conserved histidine (the H230A mutation) within a loop adjacent to the fusion loop was previously shown to block SFV fusion and infection, although the mutant E1 protein still inserts into target membranes and forms a homotrimer. Here we report on second-site mutations in E1 that rescue the H230A mutant. These mutations were located in a cluster within the hinge region, at the membrane-interacting tip, and within the groove where the E1 stem is believed to pack. Together the revertants reveal specific and interconnected aspects of the fusion protein refolding reaction.

journal_name

J Virol

journal_title

Journal of virology

authors

Chanel-Vos C,Kielian M

doi

10.1128/JVI.00167-06

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

6115-22

issue

12

eissn

0022-538X

issn

1098-5514

pii

80/12/6115

journal_volume

80

pub_type

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