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Title: 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.

Authors:
; ; ; ; ;  [1];  [2]
  1. UPENN
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
DOE - BASIC ENERGY SCIENCESNIH
OSTI Identifier:
1169999
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nat. Struct. Mol. Biol.; Journal Volume: 17; Journal Issue: (7) ; 07, 2010
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Chowdary, Tirumala K., Cairns, Tina M., Atanasiu, Doina, Cohen, Gary H., Eisenberg, Roselyn J., Heldwein, Ekaterina E., and Tufts-MED). Crystal structure of the conserved herpesvirus fusion regulator complex gH—gL. United States: N. p., 2015. Web. doi:10.1038/nsmb.1837.
Chowdary, Tirumala K., Cairns, Tina M., Atanasiu, Doina, Cohen, Gary H., Eisenberg, Roselyn J., Heldwein, Ekaterina E., & Tufts-MED). Crystal structure of the conserved herpesvirus fusion regulator complex gH—gL. United States. doi:10.1038/nsmb.1837.
Chowdary, Tirumala K., Cairns, Tina M., Atanasiu, Doina, Cohen, Gary H., Eisenberg, Roselyn J., Heldwein, Ekaterina E., and Tufts-MED). Mon . "Crystal structure of the conserved herpesvirus fusion regulator complex gH—gL". United States. doi:10.1038/nsmb.1837.
@article{osti_1169999,
title = {Crystal structure of the conserved herpesvirus fusion regulator complex gH—gL},
author = {Chowdary, Tirumala K. and Cairns, Tina M. and Atanasiu, Doina and Cohen, Gary H. and Eisenberg, Roselyn J. and Heldwein, Ekaterina E. and Tufts-MED)},
abstractNote = {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.},
doi = {10.1038/nsmb.1837},
journal = {Nat. Struct. Mol. Biol.},
number = (7) ; 07, 2010,
volume = 17,
place = {United States},
year = {Mon Feb 09 00:00:00 EST 2015},
month = {Mon Feb 09 00:00:00 EST 2015}
}