Glycoprotein B of Aujeszky's disease virus: topographical epitope mapping and epitope-specific antibody response.

A panel of 26 monoclonal antibodies (mAbs) against glycoprotein B (gB) of Aujeszky's disease (pseudorabies) virus (ADV), a glycoprotein complex consisting of three glycoproteins, gBa, gBb, and gBc, was produced by two research groups and was used for the topographical epitope mapping of gB. An epitope map was constructed in which the identified epitopes of gB were situated in 14 topologically distinct antigenic domains; ten antigenic domains represented by 22 mAbs were localized on gBc, while four antigenic domains represented by four mAbs resided on gBb of the gB complex. All the epitopes located on gBc appeared to be conformation-dependent, whereas all the epitopes on gBb were conformation-independent. The identified epitopes of gB were conserved among laboratory, vaccine and field ADV strains. Conformation-dependent epitopes were shown to contribute largely to the overall antibody response to gB in naturally infected swine and immunized mice. Moreover, it was found that most of the infected animals responded relatively weakly to the identified conformation-independent epitopes of gB, while a group of immunodominant epitopes that induced a strong antibody response was represented exclusively by conformation-dependent epitopes from different antigenic domains. The results clearly demonstrated that conformation-dependent epitopes of gBc play a crucial role in inducing the humoral immune response to gB of ADV during the natural infection of swine and immunization of mice. The application of mAbs of our panel as research and diagnostic tools is discussed.

A new monoclonal antibody detecting ochratoxin A at the picogram level.

A monoclonal antibody against ochratoxin A was produced after immunization of Balb/c mice with ochratoxin A-BSA. This antibody was of the IgG1 heavy chain subclass with a kappa type light chain. The 50% inhibition value was 0.45 ng ml-1 in a direct competitive ELISA and the detection limit was 42 pg ml-1. This antibody is very specific, cross-reacting only with ochratoxin B (9.3%).

In vitro neutralization of T-2 toxin toxicity by a monoclonal antibody.

A T-2 toxin specific monoclonal antibody, IgG1 K, with a low level of ELISA cross-reactivity to Acetyl T-2, HT-2, and iso T-2 toxins has been produced. The ability of this monoclonal antibody to neutralize the cytotoxicity of T-2 toxin in PHA stimulated cultures of human lymphocytes was determined by the MTT method. The complete neutralization of the toxic effect of 0.02 microM T-2 toxin was obtained with 0.03 microM of MoAb, whereas the 50% neutralizing dose (ND50) was observed at 0.009 microM of MoAb. Partial neutralization was observed with Acetyl T-2 toxin (ND50 = 0.038 microM) and HT-2 (ND50 = 0.94 microM). These results could represent a rational for clinical use of T-2 toxin specific monoclonal antibody in prophylaxis and therapy of T-2 toxemia.