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Type-specific reactivity of anti-glycoprotein G antibodies from herpes simplex virus-infected individuals is maintained by single or dual type-specific residues.

Review article
Authors Petra Tunbäck
Tomas Bergström
Gun-Britt Löwhagen
Johan Hoebeke
Jan-Åke Liljeqvist
Published in The Journal of general virology
Volume 86
Issue Pt 2
Pages 247-51
ISSN 0022-1317
Publication year 2005
Published at Institute of Selected Clinical Sciences, Department of Dermatology and Venereology
Institute of Laboratory Medicine, Dept of Clinical Virology
Pages 247-51
Language en
Links dx.doi.org/10.1099/vir.0.80656-0
Keywords Amino Acid Substitution, Antibodies, Viral, chemistry, immunology, Antibody Specificity, Herpes Simplex, blood, immunology, Herpesvirus 1, Human, immunology, Herpesvirus 2, Human, immunology, Humans, Models, Molecular, Molecular Sequence Data, Peptides, chemical synthesis, immunology, Viral Envelope Proteins, chemistry, immunology
Subject categories Medical and Health Sciences

Abstract

Glycoprotein G-1 (gG-1) of herpes simplex virus type 1 (HSV-1) and gG-2 of HSV-2 are the only known HSV proteins that induce type-specific human antibody responses. Recently, it was shown that purified human anti-gG-1 and anti-gG-2 antibodies presented a type-specific reactivity to immunogenic stretches with high similarity between gG-1 and gG-2. In this study, the molecular basis for this type-specific recognition was investigated employing synthetic peptides covering the indicated regions, including substitutions of the type-specific residues. The results revealed that single or dual type-specific residues localized within regions of high similarity could induce significant structural differences, explaining the type-specific recognition of the human antibody response to the gG proteins.

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