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J Gen Virol 86 (2005), 7-10; DOI 10.1099/vir.0.80567-0

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© 2005 Society for General Microbiology

Short Communication

Herpes simplex virus type 1 glycoprotein H binds to {alpha}v{beta}3 integrins

Christopher Parry{dagger}, Susanne Bell, Tony Minson and Helena Browne

Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK

Correspondence
Helena Browne
hb100{at}mole.bio.cam.ac.uk

Glycoprotein H (gH) homologues are found in all members of the herpes virus family, and gH is one of the virion envelope glycoproteins that is essential for virus entry. In this study, a recombinant soluble form of Herpes simplex virus type 1 (HSV-1) gH, in which the ectodomain is fused to the Fc-binding region of IgG, has been generated. This was expressed in mammalian cells together with gL and the resulting gHFc–gL heterodimer was purified using Protein A Sepharose. Low-affinity cell binding assays showed that gHFc–gL bound specifically to Vero cells and mutation of a potential integrin-binding motif, Arg-Gly-Asp (RGD), in gH abolished binding. CHO cells failed to bind in this assay. However, CHO cells expressing the human {alpha}v{beta}3 integrin bound efficiently to gHFc–gL, suggesting that HSV-1 gH can bind to cells using {alpha}v{beta}3 integrins and that this binding is mediated by the RGD motif in the gH ectodomain.

{dagger}Present address: Nestlé Research Centre, PO Box 44, CH-1000 Lausanne 26, Switzerland.




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