Production and characterization of monoclonal antibodies against chicken secretory IgA.

Abstract Two monoclonal antibodies (MAbs) against chicken secretory immunoglobulin A (SIgA) were generated and their binding specificities were characterized by enzyme-linked immunosorbent assay (ELISA), SDS-PAGE, and Western blotting. Analysis revealed that the subtypes of two MAbs were both IgG2b, with the light chain belonging to the kappa configuration. The affinity constant (K(aff)) of the two MAbs was 5.0 x 10(10) M(-1) and 9.7 x 10(9) M(-1), respectively. The MAbs are directed against the heavy chain domains of chicken SigA, and no cross-reactivities to IgG were observed. These results indicate that the MAbs are specific for SIgA and may be a useful tool for investigating issues regarding mucosal immunity and in the development of a good diagnostic kit for detection of specific IgA in chicken.

[Preparation and identification of the monoclonal antibody specific to hemagglutinin of avian paramyxovirus type 2].

A hybridoma cell line 1G4A7 secreting monoclonal antibody (McAb) specific to hemagglutinin of avian paramyxovirus type 2 (APMV-2) was developed by fusing the spleen cells of APMV-2 immunized BAlb/c mice with SP2/0 myeloma cells. The immunoglobulin subclass of 1G4A7 was IgG1 with light chain kappa and the affinity constant against APMV-2 was 1.02 X 10(10). Identified by HI and indirect ELISA, the McAb titers in ascities were 10 log 2 and 1 : 10(6) respectively. The McAb did not cross react with the common avian viruses, showing good specificity. There existed obvious differences in antigenitic relationship among APMV-2 viruses analyzed by HI and indirect ELISA using McAb 1G4A7.