Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 7, Pages 882-U136Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1837
Keywords
-
Funding
- US National Institutes of Health (NIH) [1DP20D001996, AI18289, AI056045, AI076231]
- Pew Scholar Program in Biomedical Sciences
- National Center for Researcher Resources at NIH [RR-15301]
- US Department of Energy, Office of Basic Energy Sciences [DE-AC02-06CH11357]
Ask authors/readers for more resources
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
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available