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Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry

Tatiana Gianni1, Raffaele Massaro1, Gabriella Campadelli-Fiume2

  • 1Department of Experimental, Diagnostic and Specialty Medicine, University of Bologna, 40126 Bologna, Italy.

Proceedings of the National Academy of Sciences of the United States of America
|July 10, 2015
PubMed

Herpes simplex virus (HSV) is an important human pathogen. It enters cells through an orchestrated process that requires four essential glycoproteins, gD, gH/gL, and gB, activated in cascade fashion by receptor-binding and signaling. gH/gL heterodimer is conserved across the Herpesviridae family. HSV entry is enabled by gH/gL interaction with αvβ6- or αvβ8-integrin receptors. We report that the interaction of virion gH/gL with integrins resulted in gL dissociation and its release in the medium. gL dissociation occurred if all components of the entry apparatus-receptor-bound gD and gB-were present and was prevented if entry was blocked by a neutralizing monoclonal antibody to gH or by a mutation in gH. We propose that (i) gL dissociation from gH/gL is part of the activation of HSV glycoproteins, critical for HSV entry; and (ii) gL is a functional inhibitor of gH and maintains gH in an inhibited form until receptor-bound gD and integrins signal to gH/gL.

Keywords:
gHgLglycoproteinherpes simplex virusvirus entry

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