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EMBO reports 7, 10, 1000–1005 (2006)
doi:10.1038/sj.embor.7400807
Molecular gymnastics at the herpesvirus surface
Félix A Rey
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Unité de Virologie Structurale and Centre National de la Recherche Scientifique, Unité de Recherche Associée 1930, Départment de Virologie, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France
Tel: +33 1 45 688563; Fax: +33 1 45 688966;
e-mail: rey@pasteur.fr
Received 16 May 2006; Accepted 21 August 2006.
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Abstract
This review analyses recent structural results that provide clues about a possible molecular mechanism for the transmission of a fusogenic signal among the envelope glycoproteins of the herpes simplex virus on receptor binding by glycoprotein gD. This signal triggers the membrane-fusion machinery of the virus—contained in glycoproteins gB, gH and gL—to induce the merging of viral and cellular membranes, and to allow virus entry into target cells. This activating process parallels that of  -retroviruses, in which receptor binding by the amino-terminal domain of the envelope protein activates the fusogenic potential of the virion in a similar way, despite the different organization of the envelope complexes of these two types of viruses. Therefore, the new structural results on the interaction of gD with its receptors might also provide insights into the mechanism of fusogenic signal transmission in -retroviruses. Furthermore, the fusion activation parallels with retroviruses, together with the recently reported structural homology of gB with the rhabdovirus envelope glycoprotein indicate that the complex entry apparatus of herpesviruses appears to be functionally related to that of simpler enveloped viruses.
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