Selective Induction of Discrete Epitopes of Herpes Simplex Virus Type 1-Specified Glycoprotein C by Interference with Terminal Steps in Glycosylation

Olofsson, Sigvard; Sjöblom, Inger; Jeansson, Stig; Datema, Roelf

doi:10.1099/0022-1317-72-8-1959

Cited by 7 publications

(6 citation statements)

References 21 publications

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“…In this case, elimination of one site of N-linked glycosylation resulted in the loss of some but not all epitopes within an antigenic site, demonstrating that altered glycosylation can have a localized effect without affecting other parts of the molecule. Investigation into the glycosylation of gC has indicated that some epitopes are dependent, some are independent, and some are masked by oligosaccharides (32,42). Site II-reactive MAbs bound to the gC-44 mutant glycoprotein normally, which confirms the independence of site II from site I.…”

Section: Discussionmentioning

confidence: 70%

Genetic analysis of type-specific antigenic determinants of herpes simplex virus glycoprotein C

Dolter

Goins

Levine

et al. 1992

J Virol

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Herpes simplex virus type 1 (HSV-1) glycoprotein C (gC-1) elicits a largely serotype-specific immune response directed against previously described determinants designated antigenic sites I and II. To more precisely define these two immunodominant antigenic regions of gC-1 and to determine whether the homologous HSV-2 glycoprotein (gC-2) has similarly situated antigenic determinants, viral recombinants

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Section: Discussionmentioning

confidence: 70%

Genetic analysis of type-specific antigenic determinants of herpes simplex virus glycoprotein C

Dolter

Goins

Levine

et al. 1992

J Virol

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“…The results show, however, that antibody responses in humans may also be elicited by the N-terminus and C-terminal intracytoplasmic domain of gC. The relatively low reactivity of human antibodies with the highly divergent portion of the N-terminus of gC-1 might reflect the clustering of O-linked carbohydrates in this region [Olofsson et al, 1991;Rux et al, 1996].…”

Section: Detection Of Linear Antigenic Determinants On Gc By Pep Scanmentioning

confidence: 79%

Mapping of linear antigenic determinants on glycoprotein C of herpes simplex virus type 1 and type 2 recognized by human serum immunoglobulin G antibodies

Ackermann

Eggers

et al. 1998

J. Med. Virol.

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Using membrane-based dekapeptides, the reactivity of human serum antibodies with linear antigenic determinants of herpes simplex virus (HSV) type 1 and type 2 glycoprotein C (gC-1, gC-2) was studied by pep scan and immunodot assay. The entire coding sequences of gC-1 and gC-2 were screened for the presence of linear epitopes by pep scan. Peptides recognized in an HSV-1 type-specific manner were mainly identified within the N-terminal third and at the C-terminus of gC-1, whereas most type-common antibodies were directed against colinear peptides within the central parts of gC-1 and gC-2. The type-specific reaction of human sera with gC-2 peptides in pep scan was poor. Eight peptides identified as immunoreactive by pep scan were further tested in immunodot assay for their reactivity with a human serum panel. None of the eight HSV-negative sera gave positive results by immunodot assay. Positive reactions with gC peptides were found to be strongly age-dependent, i.e., the rate of positive reactions was significantly higher in HSV-positive adults than in HSV-positive children. Antibody reactivity with two type-common gC peptides was demonstrated in 17 out of 28 HSV-positive sera. A putative type-specific gC-2 peptide employed in immunodot assay was inconsistently recognized by human sera. Twenty HSV-positive sera reacted with at least 1 of 5 type-specific gC-1 peptides. Nine sera showing no reactivity with glycoprotein G of HSV-1 (gG-1) by immunobloting recognized type-specific gC-1 peptides in immunodot assay. Thus, gC-1 peptides might allow the detection of HSV-1-specific antibodies in individuals showing no reactivity with commonly employed HSV-1-specific diagnostic antigenes, i.e., purified or recombinant gG-1.

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“…Anti-HSV-1 serum (K310) was produced by immunization of rabbits with sodium deoxycholate-solubilized HSV-1 membrane antigen, prepared from the F strain grown in rabbit kidney cells (26). Rabbit anti-gB (K861), anti-gC (K642), and anti-gD (K169) antisera were prepared and characterized previously (40,41). Antigens for the production of these sera as well as for the production of anti-gE (K860) rabbit antiserum and another anti-gC (K922) rabbit antiserum were prepared by immunoaffinity chromatography as described previously (41).…”

Section: Methodsmentioning

confidence: 99%

Herpes simplex virus type 1-induced hemagglutination: glycoprotein C mediates virus binding to erythrocyte surface heparan sulfate

Trybala

Svennerholm

Bergström

et al. 1993

J Virol

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We recently reported that herpes simplex virus type 1 (HSV-1) can cause agglutination of murine erythrocytes (E. Trybala, Z. Larski, and J. Wisniewski, Arch. Virol. 113:89-94, 1990). We now demonstrate that the mechanism of this hemagglutination is glycoprotein C-mediated binding of virus to heparan sulfate moieties at the surface of erythrocytes. Hemagglutination was found to be a common property of all gC-expressing laboratory strains and clinical isolates of HSV-1 tested. Mutants of HSV-1 deficient in glycoprotein C caused no specific hemagglutination, whereas their derivatives transfected with a functional gC-1 gene, thus reconstituting gC expression, regained full hemagglutinating activity. Hemagglutination activity was inhibited by antibodies against gC-1 but not by antibodies with specificity for glycoproteins gB, gD, or gE or by murine antiserum raised against the MP strain of HSV-1, which is gC deficient. Finally, purified gC-1 protein, like whole HSV-1 virions, showed high hemagglutinating activity which was inhibited by heparan sulfate and/or heparin and was completely prevented by pretreatment of erythrocytes with heparitinase, providing evidence that gC-1 mediates hemagglutination by binding to heparan sulfate at the cell surface. Thus, HSV-1-induced hemagglutination is gC-1 dependent and resembles the recently proposed mechanism by which HSV-1 attaches to surface heparans on susceptible cells, providing a simple model for initial events in the virus-cell interaction.

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Selective Induction of Discrete Epitopes of Herpes Simplex Virus Type 1-Specified Glycoprotein C by Interference with Terminal Steps in Glycosylation

Cited by 7 publications

References 21 publications

Genetic analysis of type-specific antigenic determinants of herpes simplex virus glycoprotein C

Genetic analysis of type-specific antigenic determinants of herpes simplex virus glycoprotein C

Mapping of linear antigenic determinants on glycoprotein C of herpes simplex virus type 1 and type 2 recognized by human serum immunoglobulin G antibodies

Herpes simplex virus type 1-induced hemagglutination: glycoprotein C mediates virus binding to erythrocyte surface heparan sulfate

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