Murine monoclonal antibodies (mAbs) were obtained against the outer-surface-protein OspA and OspB and against the 41-kDa flagellar antigen of Borrelia burgdorferi. The specificity of mAb was determined by the Western blotting technique and the surface association of the antigens was inferred by immunofluorescence of living bacteria. In an in vitro assay in the presence of complement, two mAbs reactive with the Ospa were able to kill borreliae, whereas several mAbs reactive with the OspA as well as with the 41-kDa flagellar protein were not. © 1992.

Cevenini R., Sambri V., Massaria F., La Placa M., Brocchi E., De Simone F. (1992). Complement-mediated in vitro bactericidal activity of monoclonal antibodies reactive with outer-surface-protein OspB of Borrelia burgdorferi. FEMS MICROBIOLOGY LETTERS, 90(2), 147-152 [10.1016/0378-1097(92)90619-Y].

Complement-mediated in vitro bactericidal activity of monoclonal antibodies reactive with outer-surface-protein OspB of Borrelia burgdorferi

Cevenini R.;Sambri V.;La Placa M.;
1992

Abstract

Murine monoclonal antibodies (mAbs) were obtained against the outer-surface-protein OspA and OspB and against the 41-kDa flagellar antigen of Borrelia burgdorferi. The specificity of mAb was determined by the Western blotting technique and the surface association of the antigens was inferred by immunofluorescence of living bacteria. In an in vitro assay in the presence of complement, two mAbs reactive with the Ospa were able to kill borreliae, whereas several mAbs reactive with the OspA as well as with the 41-kDa flagellar protein were not. © 1992.
1992
Cevenini R., Sambri V., Massaria F., La Placa M., Brocchi E., De Simone F. (1992). Complement-mediated in vitro bactericidal activity of monoclonal antibodies reactive with outer-surface-protein OspB of Borrelia burgdorferi. FEMS MICROBIOLOGY LETTERS, 90(2), 147-152 [10.1016/0378-1097(92)90619-Y].
Cevenini R.; Sambri V.; Massaria F.; La Placa M.; Brocchi E.; De Simone F.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/885427
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