Anti-idiotypic antibodies mimic bovine viral diarrhea virus antigen

Xue, Wei; Orten, Dana J.; Abdelmagid, O.Y.; Rider, Maureen A.; Blecha, Frank; Minocha, H.C.

doi:10.1016/0378-1135(91)90128-3

Cited by 16 publications

(12 citation statements)

References 23 publications

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“…The function of two proteinaceous receptor candidates is less clear. A 50-kDa protein was identified by using anti-idiotypic antibodies raised against neutralizing MAbs binding to BVDV E2 (35,36). The anti-idiotypic antibodies as well as the enriched 50-kDa protein, which is also present on cells of nonsusceptible species, were able to block BVDV infection of bovine cells (37).…”

Section: Discussionmentioning

confidence: 99%

CD46 Is a Cellular Receptor for Bovine Viral Diarrhea Virus

Maurer

Krey

Moennig

et al. 2004

J Virol

112

117

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Section: Discussionmentioning

confidence: 99%

CD46 Is a Cellular Receptor for Bovine Viral Diarrhea Virus

Maurer

Krey

Moennig

et al. 2004

J Virol

112

117

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“…The results of our studies present the first evidence that gp53, a BVDV envelope glycoprotein, binds to a cell surface receptor. First, the anti-D89 anti-id bears an internal image of a neutralizing epitope on gp53 (Xue et al, 1991) and specifically binds to bovine cell receptors for BVDV using the binding site specific for the antigen-binding site of MAb D89. Second, a cell membrane protein from MDBK cells with an approximate Mr of 50K can be immunoprecipitated by anti-D89.…”

Section: Strain Variations Of Bvdv In Attaching To Bovine Cellsmentioning

confidence: 99%

“…As described previously (Xue et al, 1991), monolayers of MDBK cells in 24-well tissue culture plates (MULTIWELL; Becton Dickinson) were treated with the anti-D89 anti-id at a concentration of 5 pg/well for 1 h at 4 °C. This amount of anti-id/well produces the highest percentage inhibition of BVDV infection of MDBK cells (Xue et al, 1991). The cells were then infected with different BVDV strains at a multiplicity of 1 for 24 h, and infected cells were detected by an indirect immunofluorescence assay as previously described (Xue et al, 1990).…”

Section: Variations Between Virus Strains In Binding To Cell Receptorsmentioning

confidence: 99%

“…We have described rabbit polyclonal anti-ids that bear the internal image of epitopes on gp53 and inhibit BVDV infection in Madin-Darby bovine kidney (MDBK) cells (Xue et al, 1991). The purposes of the present study were to look for evidence of involvement of gp53 in attachment to cell receptors, to identify the cell surface component mediating BVDV entry, and to test variations between strains of BVDV in binding to cells by using the anti-ids.…”

Section: Introductionmentioning

confidence: 99%

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Identification of the cell surface receptor for bovine viral diarrhoea virus by using anti-idiotypic antibodies

Xue

Minocha

1993

Journal of General Virology

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We have produced and characterized polyclonal antiidiotypic antibodies (anti-ids) that mimic the antigenic structures of gp53 from bovine viral diarrhoea virus (BVDV). In this study, the anti-ids were used to identify cell receptors for BVDV. The anti-ids bound specifically to bovine cells, as determined by flow cytometric analysis, and inhibitory binding assays showed that they bound to the cell surface receptors for BVDV. A cell surface protein with an M,, of approximately 50K was immunoprecipitated by the anti-ids from MDBK cells; this was blocked by preincubation of cell lysate with BVDV. This indicates that the 50K protein might be a specific receptor for BVDV gp53. Thirteen BVDV strains were used to evaluate inhibition ofanti-id binding to MDBK cells and inhibition of BVDV infection of anti-id-treated MDBK cell monolayers. Results demonstrated that both processes were inhibited to varying degrees depending on virus strain. The results suggested that multiple receptors for BVDV attachment may exist on MDBK cells, and that different virus strains do not have the same receptor.

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“…Anti-idiotypic antibodies were purified from sera obtained after the final, eighth, bleeding, according to ref. 22 Antibodies. Protein A-Sepharose affinity-purified IgG from HD1 and preimmune serum were used throughout this study.…”

Section: Methodsmentioning

confidence: 99%

Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis.

Huang¹,

Campadelli-Fiume²

1996

Proc. Natl. Acad. Sci. U.S.A.

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Glycoprotein D (gD) of herpes simplex virus 1 (HSV-1) is required for stable attachment and penetration of the virus into susceptible cells after initial binding. We derived anti-idiotypic antibodies to the neutralizing monoclonal antibody HD1 to gD of HSV-1. These antibodies have the properties expected of antibodies against a gD receptor. Specifically, they bind to the surface ofHEp-2, Vero, and HeLa cells susceptible to HSV infection and specifically react with a Mr 62,000 protein in these and other (143TK-and BHK) cell lines. They neutralize virion infectivity, drastically decrease plaque formation by impairing cell-to-cell spread of virions, and reduce polykaryocytosis induced by strain HFEM, which carries a syncytial (syn-) mutation. They do not affect HSV growth in a single-step cycle and plaque formation by an unrelated virus, indicating that they specifically affect the interaction of HSV gD with a cell surface receptor. We conclude that the Mr 62,000 cell surface protein interacts with gD to enable spread of HSV-1 from cell to cell and virusinduced polykaryocytosis.

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Anti-idiotypic antibodies mimic bovine viral diarrhea virus antigen

Cited by 16 publications

References 23 publications

CD46 Is a Cellular Receptor for Bovine Viral Diarrhea Virus

CD46 Is a Cellular Receptor for Bovine Viral Diarrhea Virus

Identification of the cell surface receptor for bovine viral diarrhoea virus by using anti-idiotypic antibodies

Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis.

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