Abstract

Eimeria tenella is a coccidian parasite of great economical importance for poultry industry. The surface of Eimeria invasive agents, sporozoites and merozoites, is coated with a family of developmentally regulated glycosylphosphatidylinositol (GPI)-linked surface antigens (SAGs), some of them involved in the initiation of the infection process. Using 2D gel electrophoresis followed by mass spectrometry, an antigenic surface protein EtSAG1 (TA4) of E. tenella sporozoites has been identified as a target of neutralizing monoclonal antibody 2H10E3. To clarify the mechanism of invasion inhibition caused by the EtSAG1-specific antibodies, a structural model of EtSAG1 was generated. It appears that "EtSAG fold" does not bear an evolutionary relationship to any known protein structure. The intra- and interchain disulfide bonds could be assigned to certain pairs of six conserved cysteines found in members of the EtSAG protein family. The outward-facing surface of the antigen was found to comprise an expanded positively charged patch, thus suggesting that the parasite invasion process may be initiated by sporozoite attachment to negatively charged sulfated proteoglycans on the surface of the host cell.