CVI
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rekabdar, E.
Right arrow Articles by Bergström, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rekabdar, E.
Right arrow Articles by Bergström, T.

 Previous Article  |  Next Article 

Clinical and Diagnostic Laboratory Immunology, November 1999, p. 826-831, Vol. 6, No. 6
1071-412X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Variability of the Glycoprotein G Gene in Clinical Isolates of Herpes Simplex Virus Type 1

Elham Rekabdar,1 Petra Tunbäck,1,2 Jan-Åke Liljeqvist,1 and Tomas Bergström1,*

Departments of Clinical Virology1 and Dermatology,2 Göteborg University, Göteborg, Sweden

Received 3 May 1999/Returned for modification 14 July 1999/Accepted 31 August 1999

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 K122 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 (F111right-arrowV) 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 F111right-arrowV 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.

* Corresponding author. Mailing address: Dept. of Clinical Virology, Guldhedsgatan 10b, S-413 46 Göteborg, Sweden. Phone: 46 31 342 47 35. Fax: 46 31 82 70 32. E-mail: Tomas.Bergstrom{at}microbio.gu.se.

Clinical and Diagnostic Laboratory Immunology, November 1999, p. 826-831, Vol. 6, No. 6
1071-412X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Antimicrob. Agents Chemother. Clin. Microbiol. Rev. Infect. Immun.
J. Clin. Microbiol. J. Virol. ALL ASM JOURNALS

Copyright © 1999 by the American Society for Microbiology. All rights reserved.