A mouse monoclonal antibody that binds to an alpha-stichocyte of Trichinella spiralis.

Monoclonal antibodies were generated for the isolation of specific antigens from Trichinella spiralis. A monoclonal antibody (TS32D12) of the IgG1 class was selected according to its reactivity and specificity by enzyme-linked immunosorbent assay and immunofluorescent technique. The TS32D12 antibody was purified from ascites by fast protein liquid chromatography. The purified antibody showed a sensitive reaction to the T. spiralis antigen, but not to any other heterologous parasite antigens so far examined. Western blot analysis showed that the monoclonal antibody bound to epitopes present on the 160-kDa molecule. The antigen molecule was fragmented into 56-kDa molecules by heat treatment. The epitopes seemed to be destroyed since the antibody could not bind to the 56-kDa molecule. Staining with the periodic acid-Schiff (PAS) reagent suggested that the two molecules of 160 kDa and 56 kDa were glycoproteins. The 160-kDa molecule was detected only in the alpha-stichocyte of T. spiralis muscle larvae.