Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL.

Abstract:

:Herpesviruses, which cause many incurable diseases, infect cells by fusing viral and cellular membranes. Whereas most other enveloped viruses use a single viral catalyst called a fusogen, herpesviruses, inexplicably, require two conserved fusion-machinery components, gB and the heterodimer gH-gL, plus other nonconserved components. gB is a class III viral fusogen, but unlike other members of its class, it does not function alone. We determined the crystal structure of the gH ectodomain bound to gL from herpes simplex virus 2. gH-gL is an unusually tight complex with a unique architecture that, unexpectedly, does not resemble any known viral fusogen. Instead, we propose that gH-gL activates gB for fusion, possibly through direct binding. Formation of a gB-gH-gL complex is critical for fusion and is inhibited by a neutralizing antibody, making the gB-gH-gL interface a promising antiviral target.

journal_name

Nat Struct Mol Biol

authors

Chowdary TK,Cairns TM,Atanasiu D,Cohen GH,Eisenberg RJ,Heldwein EE

doi

10.1038/nsmb.1837

subject

Has Abstract

pub_date

2010-07-01 00:00:00

pages

882-8

issue

7

eissn

1545-9993

issn

1545-9985

pii

nsmb.1837

journal_volume

17

pub_type

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