Russ. J. Immunol. 1997, July 15, 2 (2), 104-110.
Monoclonal antibodies to porcine IgG and light chains were produced and characterized. The specificity of selected mAbs was revealed by their selective reactivity with porcine immunoglobulins in ELISA, immunodiffusion, immunoelectrophoresis, and immunoblot analysis. For determining the presence of different IgG and light chains epitopes responsible for cross-reactivity (i.e. common epitopes) on the heterologous immunoglobulins, all mAbs were tested using sera and IgG from 12 animal species and man. All mAbs were used in unlabeled and HRP-labeled form in competitive ELISA to map the antigenic structure of the IgG and L chains. Four different epitopes shared by isotypes IgG1 and IgG2, and therefore specific for IgG class determinants, were recognized. In addition, four different epitopes specific for IgG1 were identified. Three mAbs are directed to different L-chains of porcine immunoglobulins, 2 mAbs recognized slower-migrating light chain L1, whereas one mAb reacted with the faster-migrating light chain L2 in porcine immunoglobulins. For the detection and quantitation of IgG1, a sandwich ELISA was developed. The availability of the set of mAbs to porcine immunoglobulin isotypes will stimulate and facilitate a further study of the porcine immune system.