Characterization of membrane antigens on human cytomegalovirus-infected fibroblasts recognized by human antibodies

Voort, L H van der; Leij, Lou F. de; The, T. H.

doi:10.1128/jvi.63.3.1485-1488.1989

Cited by 12 publications

(2 citation statements)

References 15 publications

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“…The detection of gp55 on the surface of infected cells was anticipated because previous studies utilizing monoclonal anti-gp55 antibodies have shown that these antibodies reacted with the surface of infected cells (35). However, the finding of gpll6 and gp170 on the cell surface was somewhat unexpected.…”

Section: Discussionmentioning

confidence: 98%

Cell surface expression of human cytomegalovirus (HCMV) gp55-116 (gB): use of HCMV-recombinant vaccinia virus-infected cells in analysis of the human neutralizing antibody response

Britt

Vugler

Butfiloski

et al. 1990

J Virol

293

121

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Cell surface expression of the human cytomegalovirus (HCMV) major envelope glycoprotein complex, gp55-116 (gB), was studied by using monoclonal antibodies and an HCMV gp55-116 (gB) recombinant vaccinia virus. HCMV-infected human fibroblasts and recombinant vaccinia virus-infected HeLa cells expressed three electrophoretically distinct proteins of Mr 170,000, 116,000, and 55,000 on their surface. These species have been previously identified within infected cells and purified virions. Two unique neutralizing epitopes were shown to be present on the cell surface gp55-116 (gB). Utilizing HeLa cells infected with the gp55-116 recombinant vaccinia virus as a specific immunosorbent, we have shown that approximately 40 to 70% of the total serum virus-neutralizing activity of a group of individuals with past HCMV infections was directed against this single envelope glycoprotein. The implications of this finding for vaccine development are discussed.

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Section: Discussionmentioning

confidence: 98%

Cell surface expression of human cytomegalovirus (HCMV) gp55-116 (gB): use of HCMV-recombinant vaccinia virus-infected cells in analysis of the human neutralizing antibody response

Britt

Vugler

Butfiloski

et al. 1990

J Virol

293

121

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“…In this investigation, the immune response to CMV gB at the clonal level is extended from the immunized mouse system to the naturally infected human host. Previously, data on the reactivity of human polyclonal antibodies against the gB antigen have been collected (3,5,19,22,26,38,48), and it has been shown that 40 to 70% of serum CMV-neutralizing activity is specific for gB (4). Three to seven epitopes have been described for the major neutralizing determinant of gp58, on the basis of studies of the murine immune response against gB (20,29,37).…”

Section: Discussionmentioning

confidence: 99%

Fine specificity of the human immune response to the major neutralization epitopes expressed on cytomegalovirus gp58/116 (gB), as determined with human monoclonal antibodies

Ohlin

Sundqvist

Mach

et al. 1993

J Virol

107

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The humoral immune response to human cytomegalovirus (CMV) membrane glycoprotein gp58/116 (gB) has been studied by establishing cell lines producing specific human monoclonal antibodies. These cell lines were generated from peripheral blood lymphocytes obtained from a healthy carrier. Hybridomas producing gp58/116-specific antibodies were detected by reactivity to procaryotically expressed proteins containing the major neutralizing epitopes of this glycoprotein complex. One antibody, ITC88, which recognized an epitope located between amino acid residues 67 and 86 of gpll6, potently neutralized the virus at 1 to 2 tLg of immunoglobulin G per ml. Only four of the six human antibodies detecting the major neutralizing domain of gp58 neutralized the virus, and none of them required complement for activity. All antibodies that bound mature, processed gp58 recognized a conformational epitope involving sequences between residues 549 and 635. However, small differences existed between the antibodies in the actual minimal requirement for Cand N-terminal parts of this epitope. By peptide mapping with several of the antibodies, the epitope was shown to

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Association of autoantibodies to myeloperoxidase with different forms of vasculitis

Tervaert

Goldschmeding

Elema

et al. 1990

Arthritis & Rheumatism

178

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Antineutrophil cytoplasmic autoantibodies with specificity for myeloperoxidase (MPO) were found in 53 patient sera that were routinely submitted for antineutrophil cytoplasmic antibody determination. Based on clinical and histologic criteria, 15 of these 53 patients were classified as having systemic necrotizing vasculitis of the polyarteritis group, 11 patients were classified as having Wegener's granulomatosis (WG), and 14 were classified as having idiopathic crescentic glomerulonephritis. The remaining 13 patients did not fulfill the diagnostic criteria for these disorders, although most of these patients had clinical symptoms compatible with these disorders. While all patients with WG had renal involvement, only 4 of the 15 patients with systemic necrotizing vasculitis of the polyarteritis group had glomerulonephritis. The sensitivity of autoantibodies to MPO for either systemic necrotizing vasculitis of the polyarteritis group, WG, or idiopathic crescentic glomerulonephritis was further tested in all our patients with these disorders (n = 104). Twenty-seven of 104 patients had autoantibodies to MPO. Furthermore, 69 of the remaining 77 patients had autoantibodies specific for the 29-kd serine protease, which has been reported to be specifically associated with WG. Sera from 8 patients were negative for either of these antibodies (92% sensitivity of autoantibodies to MPO and/or the 29-kd mine protease). The specificity of autoantibodies to MPO for either systemic necrotizing vasculitis of the polyarteritis group, WG, or idiopathic crescentic glomerulonephritis was also tested in selected groups of patients who had closely related diseases. Two of 144 patients had autoantibodies to MPO (specificity 99%). We conclude that these antibodies are not only associated with idiopathic and vasculitis-associated crescentic glomerulonephritis, but also with classic polyarteritis nodosa, Churg-Strauss syndrome, and the polyangiitis overlap syndrome without renal involvement. The presence of autoantibodies to MPO or the 29-kd serine protease is highly sensitive and specific for systemic necrotizing vasculitis of the polyarteritis group, WG, and idiopathic crescentic glomerulonephritis.The connective tissue diseases are associated with autoantibodies to various non-organ-specific antigens, particularly nuclear antigens (1). The sensitivity and specificity of these autoantibodies for certain disease entities or disease subsets are generally well delineated. In systemic necrotizing vasculitis, however, laboratory tests are generally considered nondiagnostic (2,3).During the last few years, anticytoplasmic autoantibodies or antineutrophil cytoplasmic autoantibod-

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Characterization of membrane antigens on human cytomegalovirus-infected fibroblasts recognized by human antibodies

Cited by 12 publications

References 15 publications

Cell surface expression of human cytomegalovirus (HCMV) gp55-116 (gB): use of HCMV-recombinant vaccinia virus-infected cells in analysis of the human neutralizing antibody response

Cell surface expression of human cytomegalovirus (HCMV) gp55-116 (gB): use of HCMV-recombinant vaccinia virus-infected cells in analysis of the human neutralizing antibody response

Fine specificity of the human immune response to the major neutralization epitopes expressed on cytomegalovirus gp58/116 (gB), as determined with human monoclonal antibodies

Association of autoantibodies to myeloperoxidase with different forms of vasculitis

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