Abstract
Apicomplexans are a group of parasitic protozoans, including Plasmodium and Cryptosporidium species, which harbor a specialized organelle called an apicoplast. Of the 145-apicomplexan lineage-specific proteins identified in Cryptosporidium parvum, 30 are surface proteins. In Plasmodium falciparum, a heteromeric complex of three related apicomplexan lineage-specific membrane proteins containing 6 transmembrane domains (m6t) have been identified. These proteins are Pfm6t α, Pfm6t β, and Pfm6t γ and these proteins are localized on merozoite as an inner membrane complex (Rayavara et al. in Mol Biochem Parasitol 167(2):135-143, 2009). In C. parvum, homologs of these proteins are identified and are Cpm6t α, Cpm6t β, and Cpm6t γ. Mass spectrometric analysis of C. parvum (Iowa II) protein extracts of oocyst, sporozoite and soluble and insoluble fractions of cytoplasm identified the presence of Cpm6t α, Cpm6t β, and Cpm6t γ specific peptides in these fractions. The expression of Cpm6t α, Cpm6t β, and Cpm6t γ proteins on various developmental stages of C. parvum suggests that this novel group of apicomplexan lineage-specific proteins in Cryptosporidium may be involved in multiple cellular processes apart from the invasion into host epithelial cells as suggested for P. falciparum merozoites onto host erythrocytes.