4.4 Article

Human antibodies to herpes simplex virus type 1 glycoprotein C are neutralizing and target the heparan sulfate-binding domain

Journal

VIROLOGY
Volume 400, Issue 2, Pages 197-206

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.01.032

Keywords

Herpes simplex virus type 1; Glycoprotein gC; Anti-gC antibody; Virus-neutralizing activity; Glycosaminoglycans

Categories

Funding

  1. Glycoconjugates in Biological Systems
  2. Swedish Medical Research Council [11225]
  3. Sahlgren's University Hospital Lakarutbildningsavtal (LUA)
  4. Scandinavian Society for Antimicrobial Chemotherapy

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Human antibodies specific for glycoprotein C (gC1) of herpes simplex virus type 1 (HSV-1) neutralized the virus infectivity and efficiently inhibited attachment of HSV-1 to human HaCaT keratinocytes and to murine mutant L cells expressing either heparan sulfate or chondroitin sulfate at the cell surface. Similar activities were observed with anti-gC1 monoclonal antibody B1C1. In addition to HaCaT and L cells, B1C1 antibody neutralized HSV-1 infectivity in simian GMK AH1 cells mildly pre-treated with heparinase III. Human anti-gC1 antibodies efficiently competed with the binding of gC1 to B1C1 antibody whose epitope overlaps a part of the attachment domain of gC1. Human anti-gC1 and B1C1 antibodies extended survival time of mice experimentally infected with HSV-1. We conclude that in HaCaT cells and in cell systems showing restricted expression of glycosaminoglycans, human and some monoclonal anti-gC1 antibodies can target the cell-binding domain of this protein and neutralize viral infectivity. (C) 2010 Elsevier Inc. All rights reserved.

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