The Identification, Expression, And. Immunological Characterization Of A Member Of The Profilin Family

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4. Discussion The present study describes the identification, expression, and immunological characterization of a member of the profilin family from three pathogenic Babesia species. The deduced amino acid sequence of PROFs from B. bigemina and B. microti is similar to those of other known apicomplexan parasites consisting of polypeptide binding and putative PIP2-interaction sites, profilin family domain, and GlcNAc glycosylation sites (Yarovinsky et al., 2005, 2006; Kursula et al., 2008; Kucera et al., 2010; Jenkins et al., 2010). A phylogenetic analysis revealed that PROF of Babesia species was clustered into a clade closely related to the PROF from other piroplasmids (identities 39.9e73.6% and similarities 55.9e80.5%), indicating that PROF of B. bovis, B. bigemina and B. microti possess a function similar to those of piroplasmids’PROF. The recombinant PROFs of B. bovis, B. bigemina, and B. microti were successfully produced as soluble GST fusion proteins, and they were found to cross-react. A high degree of homology may explain the serological cross-reactivity between the PROF proteins of B. bovis, B. bigemina, and B. microti. Another possible explanation is Babeisa PROF proteins share immunodominant epitopes and raises the possibility that such epitopes may be involved in a crossprotective immune response. Further, using anti-rPROFs mice sera, a native PROF proteins were observed in cytoplasm of the Babesia merozoites, suggesting that PROF proteins are shared antigens

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