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Variability of the glycoprotein G gene in clinical isolates of herpes simplex virus type 1.

Journal article
Authors Elham Rekabdar
Petra Tunbäck
Jan-Åke Liljeqvist
Tomas Bergström
Published in Clinical and diagnostic laboratory immunology
Volume 6
Issue 6
Pages 826-31
ISSN 1071-412X
Publication year 1999
Published at Institute of Selected Clinical Sciences, Department of Dermatology and Venereology
Institute of Laboratory Medicine, Dept of Clinical Virology
Pages 826-31
Language en
Links www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Adult, Aged, Amino Acid Sequence, Amino Acid Substitution, Animals, Antibodies, Monoclonal, Antibodies, Viral, immunology, Antigens, Surface, analysis, immunology, Cells, Cultured, Cercopithecus aethiops, DNA Mutational Analysis, DNA, Viral, analysis, Enzyme-Linked Immunosorbent Assay, Epitopes, immunology, Female, Genetic Variation, Herpes Simplex, genetics, immunology, Herpesvirus 1, Human, genetics, immunology, Humans, Immunoglobulin G, immunology, Kidney, cytology, Male, Middle Aged, Molecular Sequence Data, Polymerase Chain Reaction, Sensitivity and Specificity, Serologic Tests, Viral Envelope Proteins, genetics, immunology
Subject categories Dermatology and Venereal Diseases

Abstract

Glycoprotein G (gG) of herpes simplex virus type 1 (HSV-1) has been used as a prototype antigen for HSV-1 type-specific serodiagnosis, but data on the sequence variability of the gene coding for this protein in wild-type strains are lacking. In this study, direct DNA sequencing of the gG-1 genes from PCR products was performed with clinical HSV-1 isolates from 11 subjects as well as with strains Syn 17(+), F, and KOS 321. The reference strains Syn 17(+) and F showed a high degree of conservation, while KOS 321 carried 13 missense mutations and, in addition, 12 silent mutations. Three clinical isolates showed mutations leading to amino acid alterations: one had a mutation of K(122) to N, which is a gG-1-to-gG-2 alteration; another contained all mutations which were observed in KOS 321 except two silent mutations; and the third isolate carried five missense mutations. Two clinical isolates as well as strain KOS 321 showed a mutation (F(111)-->V) within the epitope of a gG-1-reactive monoclonal antibody (MAb). When all viruses were tested for reactivity with the anti-gG-1 MAb, the three strains with the F(111)-->V mutation were found to be unreactive. Furthermore, gG-1 antibodies purified from sera from the two patients carrying strains mutated in this epitope were less reactive when they were tested by an HSV-1-infected-cell assay. Therefore, our finding that the sequence variability of the gG-1 gene also affects B-cell epitope regions of this protein in clinical isolates may have consequences for the use of this protein as a type-specific antigen for serodiagnosis.

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