Characterization of a Major Antigenic Region on gp55 of Human Cytomegalovirus

Silvestri, Michel; Sundqvist, Vivi‐Anne; Rudén, Ulla; Wahrén, Britta

doi:10.1099/0022-1317-72-12-3017

Cited by 23 publications

(20 citation statements)

References 34 publications

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“…Much work has been directed at defining immunologically relevant epitopes on the protein (for example see Silvestri et al, 1991). These reports have been abstracted as MAb reactivities in Table 2.…”

Section: R R Spaete R C Gehrz and M P Landinimentioning

confidence: 99%

Human cytomegalovirus structural proteins

Spaete¹,

Gehrz²,

Landini³

1994

Journal of General Virology

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Section: R R Spaete R C Gehrz and M P Landinimentioning

confidence: 99%

Human cytomegalovirus structural proteins

Spaete¹,

Gehrz²,

Landini³

1994

Journal of General Virology

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“…These studies indicate that certain regions of the molecule are immunodominant in humans [Kniess et al, 1991;Silvestri et al, 1991;Utz et al, 1989;Wagner et al, 1992]. Following immunization with a live HCMV vaccine or a subunit gB vaccine, both recipients have IgG and secretory IgA to HCMV gB with comparable levels of virus neutralizing activity .…”

Section: Introductionmentioning

confidence: 99%

Humoral immune response to functional regions of human cytomegalovirus glycoprotein B

et al. 1997

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Sera from patients with primary human cytomegalovirus (HCMV) infections, both acute and convalescent phase, and from HCMV-seropositive healthy subjects were analyzed to determine whether the sera would recognize antigenic domains on HCMV glycoprotein B (gB) that function in virion infectivity and spread of virus from cell to cell. The intact gB molecule, amino-terminal derivatives of different lengths, and internal deletion derivatives were expressed in eukaryotic cells and reacted by immunofluorescence with the sera. All convalescent-phase sera and most sera from healthy seropositive individuals reacted with full-length gB and with an amino-terminal derivative containing 687 amino acids (aa), gB-(1-687); approximately half of the sera recognized an amino-terminal derivative of 447 aa, gB-(1-447), and one-third reacted with the shortest deletion derivative of 258 aa, gB-(1-258). Of the acute-phase sera, 77% recognized intact gB and gB-(1-687), 32% recognized gB-(1-447), and 14% recognized gB-(1-258). Deletion of aa 548 to 618 dramatically reduced the percentage of reactive sera, whereas deletion of aa 411 to 447 had a minor impact on reactivity of sera. To investigate the epitope specificity of human antibodies to gB, we carried out competition experiments between human sera with neutralizing activity and selected monoclonal antibodies (mAbs) to conformational epitopes on gB. We found that antibodies in human sera preclude syncytium formation in UB15-11 glioblastoma cells constitutively expressing gB and compete with certain murine mAbs that block virus entry into cells and transmission of infection from cell to cell. Our results show that HCMV-immune human sera contain antibodies to functional regions on gB, and the abundance of these antibodies in convalescent-phase sera suggests that they may play a central role in limiting dissemination of virus in the host.

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“…Gp58 represents the C-terminal part of the precursor protein and most likely functions as the transmembrane protein, whereas gpll6 corresponds to the N-terminal half (Mach et al, 1986;Meyer et al, 1990;Kari et al, 1990). Studies utilizing immunoblot analyses of prokaryotic fusion proteins and human convalescent sera have revealed that only a limited number of linear antibody binding sites is present on the H. Meyer and others gp58/116 gene product (Meyer et al, 1990;Kniess et al, 1991 ;Silvestri et al, 1991). Three major sites have been identified.…”

Section: Introductionmentioning

confidence: 99%

Glycoprotein gp116 of human cytomegalovirus contains epitopes for strain-common and strain-specific antibodies

Meyer

Sundqvist

Pereira

et al. 1992

Journal of General Virology

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109

111

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Glycoprotein gpll6 of human cytomegalovirus (HCMV) is a target for neutralizing antibodies. Gp 116 is a component of the gCI complex which consists of gp58 and gp116. Like its homologue, glycoprotein B of herpes simplex virus type 1, gp116 contains a highly antigenic region in the N-terminal part of the molecule, between amino acids 28 and 84. Prokaryotic expression plasmids and synthetic peptides were used to define binding sites for mouse and human monoclonal antibodies (MAbs) as well as HCMV convalescent sera. Site I, located between amino acids 68 and 77, contains an epitope recognized by the human MAb C23, which is capable of neutralizing HCMV independently of complement and the site is conserved between HCMV strains. Of HCMV-positive human sera, 53% recognized site I. Site II was mapped using mouse MAbs as well as human sera. It is located between residues 50 and 54, an area which is not conserved between strains AD169 and Towne, the two laboratory strains of known sequence. Strain-specific antibodies were detected in 25% of human sera. Site lI-specific antibodies, purified from human sera by affinity chromatography, were found to be incapable of neutralizing HCMV in tissue culture.

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Characterization of a Major Antigenic Region on gp55 of Human Cytomegalovirus

Cited by 23 publications

References 34 publications

Human cytomegalovirus structural proteins

Human cytomegalovirus structural proteins

Humoral immune response to functional regions of human cytomegalovirus glycoprotein B

Glycoprotein gp116 of human cytomegalovirus contains epitopes for strain-common and strain-specific antibodies

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