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Human babesiosis caused by the intraerythrocytic apicomplexan  Babesia microti  is an expanding tick-borne zoonotic disease that may cause severe symptoms and death in elderly or immunocompromised individuals. In light of an increasing resistance of  B. microti  to drugs, there is a lack of therapeutic alternatives. Species-specific proteases are essential for parasite survival and possible chemotherapeutic targets. However, the repertoire of proteases in  B. microti  remains poorly investigated. Herein, we employed several combined bioinformatics tools and strategies to organize and identify genes encoding for the full repertoire of proteases in the  B. microti  genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine ( n  = 28), serine ( n  = 21), threonine ( n  = 14), asparagine ( n  = 7), and metallopeptidases ( n  = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of  B. bovis  and  B. microti  proteases revealed differences among sensu stricto and sensu lato  Babesia  parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of  Babesia  parasites and to explore proteases as targets for developing novel therapeutic interventions.

In Silico Survey and Characterization of Babesia microti Functional and Non-Functional Proteases