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Five monoclonal antibodies (MAbs) were partially characterized and tested for their ability to inhibit penetration of Madin-Darby bovine kidney (MDBK) cells by sporozoites of Eimeria bovis. By indirect fluorescent-antibody assays, all MAbs reacted with acetone-fixed sporozoites, but only two MAbs, EbS9 (immunoglobulin G1) and EbS11 (immunoglobulin G2a), localized specifically on the plasmalemma of live sporozoites. Two of the five MAbs also reacted with acetone-fixed first-generation merozoites of E. bovis; however, none of the MAbs reacted with live merozoites. Treatment of live sporozoites with EbS9 or EbS11 resulted in 79 and 73% decreases, respectively, in sporozoite penetration of MDBK cells. No significant differences in cell penetration occurred in MDBK cells inoculated with sporozoites that had been treated with the other three MAbs. Both EbS9 and EbS11 reacted in Western blots (immunoblots) of sporozoites with the same 20,000-relative-molecular-weight protein. The antigens against which these neutralizing MAbs react might be useful in immunizing against bovine coccidiosis.

infection and immunity

Inhibition of penetration of cultured cells by Eimeria bovis sporozoites by monoclonal immunoglobulin G antibodies against the parasite surface protein P20