Crystal structure of the conserved herpes virus fusion regulator complex gH-gL

Journal Article · Mon Sep 13 04:00:00 EDT 2010 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.1837· OSTI ID:1018560

Chowdary, Tirumala K; Cairns, Tina M; Atanasiu, Doina; Cohen, Gary H; Eisenberg, Roselyn J; Heldwein, Ekaterina E ^[1]

---

1. UPENN

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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE Office of Science (SC)
• OSTI ID: 1018560
• Journal Information: Nature Structural & Molecular Biology, Journal Name: Nature Structural & Molecular Biology Journal Issue: (7) ; 07, 2010 Vol. 17; ISSN 1545-9993
• Publisher: Nature Publishing Group
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
CATALYSTS
CRYSTAL STRUCTURE
DISEASES
HERPES SIMPLEX
MEMBRANES
VIRUSES