Journal of General Virology, Vol 80, 1789-1798, Copyright © 1999 by Society for General Microbiology

ARTICLES

Identification of type-specific domains within glycoprotein G of herpes simplex virus type 2 (HSV-2) recognized by the majority of patients infected with HSV-2, but not by those infected with HSV-1

A Grabowska, C Jameson, P Laing, S Jeansson, E Sjogren-Jansson, J Taylor, A Cunningham and WL Irving
Department of Microbiology, University Hospital, Queen's Medical Centre, Nottingham, UK

A combination of phage peptide display library mapping and pepscanning, with both murine monoclonal antibodies and a panel of well-characterized human sera, have been used in order to define type-specific epitopes of glycoprotein G of herpes simplex virus type 2 (HSV-2) (gG2). Both techniques revealed an immunodominant region of gG2, centred around amino acids 525--587 of the uncleaved gG2 molecule. A soluble peptide, equivalent to amino acids 551--570, when used as antigen in an ELISA format was recognized by three out of five murine MAbs and by 20/26 (77%) Western blot anti-HSV-2-positive human sera, but by only 1/63 Western blot anti-HSV-2-negative sera (specificity, 98%). The sensitivity of detection of human anti-HSV-2 antibodies was increased to 90% using a peptide derived from this region, presented on a nitrocellulose membrane. This highly antigenic and type-specific domain of gG2 is located at the junction between the 'unique' region of gG2 and its C-terminal end, which has approximately 50% identity with gG1. A second antigenic region of gG2, amino acids 351--427, which lies within the 'unique' part of gG2, was also identified by both techniques employed in this study and is recognized by a proportion of anti-HSV-2-positive sera. These findings demonstrate the feasibility of developing a peptide-based type-specific assay for the detection of anti-HSV-2 antibody in human sera based on type-specific epitopes of gG2 and have implications for the understanding of the three-dimensional topography of gG2.

This article has been cited by other articles:

				K. L. Mansfield, N. Johnson, and A. R. Fooks Identification of a conserved linear epitope at the N terminus of the rabies virus glycoprotein J. Gen. Virol., November 1, 2004; 85(11): 3279 - 3283. [Abstract] [Full Text] [PDF]

				S. Q. Wales, C. C. Smith, M. Wachsman, G. Calton, and L. Aurelian Performance and Use of a Ribonucleotide Reductase Herpes Simplex Virus Type-Specific Serological Assay Clin. Vaccine Immunol., January 1, 2004; 11(1): 42 - 49. [Abstract] [Full Text] [PDF]

				M. Ikoma, J.-A. Liljeqvist, J. Groen, K. L. Glazenburg, T. H. The, and S. Welling-Wester Use of a Fragment of Glycoprotein G-2 Produced in the Baculovirus Expression System for Detecting Herpes Simplex Virus Type 2-Specific Antibodies J. Clin. Microbiol., July 1, 2002; 40(7): 2526 - 2532. [Abstract] [Full Text] [PDF]

				J.-A. Liljeqvist, B. Svennerholm, and T. Bergström Conservation of Type-Specific B-Cell Epitopes of Glycoprotein G in Clinical Herpes Simplex Virus Type 2 Isolates J. Clin. Microbiol., December 1, 2000; 38(12): 4517 - 4522. [Abstract] [Full Text]

				P. Tunbäck, J.-A. Liljeqvist, G.-B. Löwhagen, and T. Bergström Glycoprotein G of herpes simplex virus type 1: identification of type-specific epitopes by human antibodies J. Gen. Virol., April 1, 2000; 81(4): 1033 - 1040. [Abstract] [Full Text]