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Background  Cysteine proteases have been shown to be highly relevant for Apicomplexan parasites. In the case of  Babesia bovis , a tick-transmitted hemoparasite of cattle, inhibitors of these enzymes were shown to hamper intraerythrocytic replication of the parasite, underscoring their importance for survival.    Results  Four papain-like cysteine proteases were found to be encoded by the  B. bovis  genome using the MEROPS database. One of them, the ortholog of  Plasmodium falciparum  falcipain-2, here named bovipain-2, was further characterized. Bovipain-2 is encoded in  B. bovis  chromosome 4 by an ORF of 1.3 kb, has a predicted molecular weight of 42 kDa, and is hydrophilic with the exception of a transmembrane region. It has orthologs in several other apicomplexans, and its predicted amino acid sequence shows a high degree of conservation among several  B. bovis  isolates from North and South America. Synteny studies demonstrated that the  bovipain-2  gene has expanded in the genomes of two related piroplasmids,  Theileria parva  and  T. annulata , into families of 6 and 7 clustered genes respectively. The  bovipain-2 g ene is transcribed in  in vitro  cultured intra-erythrocyte forms of a virulent and an attenuated  B. bovis  strain from Argentina, and has no introns, as shown by RT-PCR followed by sequencing. Antibodies against a recombinant form of bovipain-2 recognized two parasite protein bands of 34 and 26 kDa, which coincide with the predicted sizes of the pro-peptidase and mature peptidase, respectively. Immunofluorescence studies showed an intracellular localization of bovipain-2 in the middle-rear region of  in vitro  cultured merozoites, as well as diffused in the cytoplasm of infected erythrocytes. Anti-bovipain-2 antibodies also reacted with  B. bigemina -infected erythrocytes giving a similar pattern, which suggests cross-reactivity among these species. Antibodies in sera of two out of six  B. bovis -experimentally infected bovines tested, reacted specifically with recombinant bovipain-2 in immunoblots, thus demonstrating expression and immunogenicity during bovine-infecting stages.    Conclusions  Overall, we present the characterization of bovipain-2 and demonstrate its  in vitro  and  in vivo  expression in virulent and attenuated strains. Given the involvement of apicomplexan cysteine proteases in essential parasite functions, bovipain-2 constitutes a new vaccine candidate and potential drug target for bovine babesiosis.

Bovipain-2, the falcipain-2 ortholog, is expressed in intraerythrocytic stages of the tick-transmitted hemoparasite Babesia bovis