Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection

Journal Article · Tue Apr 10 00:00:00 EDT 2007 · Virology

DOI:https://doi.org/10.1016/j.virol.2006.10.039· OSTI ID:20977014

Tsvitov, Marianna ^[1]; Frampton, Arthur R ^[1]; Shah, Waris A ^[1]; Wendell, Steven K ^[1]; Ozuer, Ali ^[1]; Kapacee, Zoher ^[1]; Goins, William F ^[1]; Cohen, Justus B ^[1]; Glorioso, Joseph C ^[1]

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1. Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, E1246 Biomedical Science Tower, Pittsburgh, PA 15261 (United States)

Herpes simplex virus type 1 (HSV-1) entry into permissive cells involves attachment to cell-surface glycosaminoglycans (GAGs) and fusion of the virus envelope with the cell membrane triggered by the binding of glycoprotein D (gD) to cognate receptors. In this study, we characterized the observation that soluble forms of the gD ectodomain (sgD) can mediate entry of gD-deficient HSV-1. We examined the efficiency and receptor specificity of this activity and used sequential incubation protocols to determine the order and stability of the initial interactions required for entry. Surprisingly, virus binding to GAGs did not increase the efficiency of sgD-mediated entry and gD-deficient virus was capable of attaching to GAG-deficient cells in the absence of sgD. These observations suggested a novel binding interaction that may play a role in normal HSV infection.

• OSTI ID: 20977014
• Journal Information: Virology, Vol. 360, Issue 2; Other Information: DOI: 10.1016/j.virol.2006.10.039; PII: S0042-6822(06)00785-9; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CELL MEMBRANES
EFFICIENCY
GLYCOPROTEINS
HERPES SIMPLEX
RECEPTORS
VIRUSES