Crystal Structure of the Conserved Herpes Virus Fusion Regulator Complex gH–gL

Journal Article · Fri Jan 01 04:00:00 EST 2010 · Nature Structural and Molecular Biology

DOI:https://doi.org/10.1038/nsmb.1837· OSTI ID:1019889

Chowdary, T; Cairns, T; Atanasiu, D; Cohen, G; Eisenberg, R; Heldwein, E

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: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: DOE - OFFICE OF SCIENCE
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 1019889
• Report Number(s): BNL--95735-2011-JA
• Journal Information: Nature Structural and Molecular Biology, Journal Name: Nature Structural and Molecular Biology Journal Issue: 7 Vol. 17; ISSN 1545-9993
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
CATALYSTS
CRYSTAL STRUCTURE
DISEASES
HERPES SIMPLEX
MEMBRANES
VIRUSES
national synchrotron light source