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Journal of Virology, June 2005, p. 7042-7049, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.7042-7049.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Heptad Repeat in Herpes Simplex Virus 1 gH, Located Downstream of the {alpha}-Helix with Attributes of a Fusion Peptide, Is Critical for Virus Entry and Fusion

Tatiana Gianni, Laura Menotti, and Gabriella Campadelli-Fiume*

Department of Experimental Pathology, Section on Microbiology and Virology, Alma Mater Studiorum, University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy

Received 9 November 2004/ Accepted 25 January 2005

Entry of herpes simplex virus 1 (HSV-1) into cells occurs by fusion with cell membranes; it requires gD as the receptor binding glycoprotein and the trigger of fusion, and the trio of the conserved glycoproteins gB, gH, and gL to execute fusion. Recently, we reported that the ectodomain of HSV-1 gH carries a hydrophobic {alpha}-helix (residues 377 to 397) with attributes of an internal fusion peptide (T. Gianni, P. L. Martelli, R. Casadio, and G. Campadelli-Fiume, J. Virol. 79:2931-2940, 2005). Downstream of this {alpha}-helix, a heptad repeat (HR) with a high propensity to form a coiled coil was predicted between residues 443 and 471 and was designated HR-1. The simultaneous substitution of two amino acids in HR-1 (E450G and L453A), predicted to abolish the coiled coil, abolished the ability of gH to complement the infectivity of a gH-null HSV mutant. When coexpressed with gB, gD, and gL, the mutant gH was unable to promote cell-cell fusion. These defects were not attributed to a defect in heterodimer formation with gL, the gH chaperone, or in trafficking to the plasma membrane. A 25-amino-acid synthetic peptide with the sequence of HR-1 (pep-gHwt25) inhibited HSV replication if present at the time of virus entry into the cell. A scrambled peptide had no effect. The effect was specific, as pep-gHwt25 did not reduce HSV-2 and pseudorabies virus infection. The presence of a functional HR in the HSV-1 gH ectodomain strengthens the view that gH has attributes typical of a viral fusion glycoprotein.

* Corresponding author. Mailing address: Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy. Phone: 39 051 2094733 or -2094734. Fax: 39 051 2094735. E-mail: gabriella.campadelli{at}unibo.it.

Journal of Virology, June 2005, p. 7042-7049, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.7042-7049.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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