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Updated: Feb 7, 2026

Plaquing of Herpes Simplex Viruses
Published on: November 5, 2021
Human antibodies to herpes simplex virus type 1 glycoprotein C are neutralizing and target the heparan
Beata Adamiak1, Edward Trybala, Kristina Mardberg
1Department of Clinical Virology, University of Gothenburg, S-413 46 Göteborg, Sweden. beata.adamiak@microbio.gu.se
Abstract:
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.
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