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Dichotomy of glycoprotein g gene in herpes simplex virus type 1 isolates.

Journal article
Authors Elham Rekabdar
Petra Tunbäck
Jan-Åke Liljeqvist
Magnus Lindh
Tomas Bergström
Published in Journal of clinical microbiology
Volume 40
Issue 9
Pages 3245-51
ISSN 0095-1137
Publication year 2002
Published at Institute of Selected Clinical Sciences, Department of Dermatology and Venereology
Institute of Laboratory Medicine, Dept of Clinical Virology
Pages 3245-51
Language en
Keywords Amino Acid Sequence, Antibodies, Monoclonal, immunology, Antibodies, Viral, immunology, Cell Line, Enzyme-Linked Immunosorbent Assay, Frameshift Mutation, Genetic Variation, Herpes Simplex, virology, Herpesvirus 1, Human, classification, genetics, immunology, Humans, Immunodominant Epitopes, Molecular Sequence Data, Sequence Analysis, DNA, Viral Envelope Proteins, chemistry, genetics, immunology
Subject categories Dermatology and Venereal Diseases


Herpes simplex virus type 1 (HSV-1) encodes 11 envelope glycoproteins, of which glycoprotein G-1 (gG-1) induces a type-specific antibody response. Variability of the gG-1 gene among wild-type strains may be a factor of importance for a reliable serodiagnosis and typing of HSV-1 isolates. Here, we used a gG-1 type-specific monoclonal antibody (MAb) to screen for mutations in the immunodominant region of this protein in 108 clinical HSV-1 isolates. Of these, 42 isolates showed no reactivity to the anti-gG-1 MAb. One hundred five strains were further examined by DNA sequencing of the middle part of the gG-1 gene, encompassing 106 amino acids including the immunodominant region and epitope of the anti-gG-1 MAb. By phylogenetic comparisons based on the sequence data, we observed two (main) genetic variants of the gG-1 gene among the clinical isolates corresponding to reactivity or nonreactivity to the anti-gG-1 MAb. Furthermore, four strains appeared to be recombinants of the two gG-1 variants. In addition, one strain displayed a gG-1-negative phenotype due to a frameshift mutation, in the form of insertion of a cytosine nucleotide. When immunoglobulin G reactivity to HSV-1 in sera from patients infected with either of the two variants was investigated, no significant differences were found between the two groups, either in a type-common enzyme-linked immunosorbent assay (ELISA) or in a type-specific gG-1 antigen-based ELISA. Despite the here-documented existence of two variants of the gG-1 gene affecting the immunodominant region of the protein, other circumstances, such as early phase of infection, might be sought for explaining the seronegativity to gG-1 commonly found in a proportion of the HSV-1-infected patients.

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