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J. Biol. Chem., Vol. 280, Issue 31, 28632-28643, August 5, 2005

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Fusogenic Domains in Herpes Simplex Virus Type 1 Glycoprotein H^*

Stefania Galdiero¶, Annarita Falanga||, Mariateresa Vitiello||, Helena Browne**, Carlo Pedone¶, and Massimiliano Galdiero

From the Department of Biological Sciences, Division of Biostructures, and the Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples "Federico II," and the ^¶Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, 80134 Naples, Italy, the Departments of ^||Pathology and Experimental Medicine, II University of Naples, Via de Crecchio 7, 80138 Naples, Italy, and the ^**Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom

Infection of eukaryotic cells by enveloped viruses requires fusion between the viral envelope and the cellular plasma or endosomal membrane. The actual merging of the two membranes is mediated by viral envelope glycoproteins, which generally contain a highly hydrophobic region termed the fusion peptide. The entry of herpesviruses is mediated by three conserved proteins: glycoproteins B, H (gH), and L. However, how fusion is executed remains unknown. Herpes simplex virus type 1 gH exhibits features typical of viral fusion glycoproteins, and its ectodomain seems to contain a putative internal fusion peptide. Here, we have identified additional internal segments able to interact with membranes and to induce membrane fusion of large unilamellar vesicles. We have applied the hydrophobicity-at-interface scale proposed by Wimley and White (Wimley, W. C., and White, S. H. (1996) Nat. Struct. Biol. 3, 842-848) to identify six hydrophobic stretches within gH with a tendency to partition into the membrane interface, and four of them were able to induce membrane fusion. Experiments in which equimolar mixtures of gH peptides were used indicated that different fusogenic regions may act in a synergistic way. The functional and structural characterization of these segments suggests that herpes simplex virus type 1 gH possesses several fusogenic internal peptides that could participate in the actual fusion event.

Received for publication, May 11, 2005 , and in revised form, June 2, 2005.

^* This work was supported by European Union Contract QLK2-CT-2002-00810. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Experimental Medicine, II University of Naples, Via de Crecchio 7, 80138 Naples, Italy. Tel.: 39-81-566-7646; Fax: 39-81-566-7578; E-mail: massimiliano.galdiero{at}unina2.it.

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