Crystal structure of the
conserved herpesvirus fusion regulator complex gH-gL
Chowdary TK, Cairns TM, Atanasiu D, Cohen GH, Eisenberg
RJ, Heldwein EE.
Nat Struct Mol Biol, 17:882-888, 2010
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.