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

Journal article
Authors Beata Adamiak
Edward Trybala
K. Mardberg
M. Johansson
Jan-Åke Liljeqvist
Sigvard Olofsson
A. Grabowska
K. Bienkowska-Szewczyk
B. Szewczyk
Tomas Bergström
Published in Virology
Volume 400
Issue 2
Pages 197-206
ISSN 0042-6822
Publication year 2010
Published at Institute of Biomedicine
Institute of Biomedicine, Department of Microbiology and Immunology
Institute of Biomedicine, Department of Infectious Medicine
Pages 197-206
Language en
Links dx.doi.org/10.1016/j.virol.2010.01....
Keywords Animals, Antibodies, Neutralizing/*immunology, Antibodies, Viral/*immunology, Binding Sites, Cell Line, Cercopithecus aethiops, Disease Models, Animal, Epitopes/immunology, Heparitin Sulfate/metabolism, Herpes Simplex/immunology, Herpesvirus 1, Human/*immunology, Humans, Keratinocytes/virology, Mice, Neutralization Tests, Survival Analysis, Viral Envelope Proteins/*immunology, Virus Attachment
Subject categories Microbiology in the medical area

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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