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Curr Opin Virol. 2013 Feb;3(1):13-9. doi: 10.1016/j.coviro.2012.10.005. Epub 2012 Oct 26.

Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry.

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Department of Molecular Biology and Microbiology and Graduate Program in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, MA 02111, United States.


Enveloped viruses enter cells by fusing the viral and cellular membranes, and most use a single viral envelope protein that combines receptor-binding and fusogenic functions. In herpesviruses, these functions are distributed among multiple proteins: the conserved fusion protein gB, various non-conserved receptor-binding proteins, and the conserved gH/gL heterodimer that curiously lacks an apparent counterpart in other enveloped viruses. Recent structural studies of gH/gL from HSV-2 and EBV revealed a unique complex with no structural or functional similarity to other viral proteins. Here we analyzed gH/gL structures and highlighted important functional regions. We propose that gH/gL functions as an adaptor that transmits the triggering signals from various non-conserved inputs to the highly conserved fusion protein gB.

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