The oligopeptidase B serine protease is an important virulence factor and therapeutic target in Trypanosoma infections. Recently, the Leishmania major Genome Project identified a new oligopeptidase B that was denominated oligopeptidase B-like, herein named oligopeptidase B-2. In this study, a complete open reading frame of oligopeptidase B-2 from Leishmania amazonensis (PH8 strain) was amplified by PCR using primers designed for the oligopeptidase B-2 gene of L. major. The 2,715 bp fragment coded for a protein of 905 amino acids with a predicted molecular mass of 103,918.9 Da and theoretical pI of 5.82. The encoded protein displayed ∼96% identity with L. major and ∼75% identity with Trypanosoma cruzi and T. brucei oligopeptidases B-2, and ∼21% identity with Escherichia coli and L. amazonensis classical oligopeptidase B. An unusual C-terminal extension was found in relation to the classical trypanosomatid oligopeptidase B. By sequence alignment, we determined a catalytic triad (Ser 629, Asp 717 and His 758), S1 subsite (Glu 674 and Glu 676) and suggest a difference in the S2 subsite of L. amazonensis oligopeptidase B-2. We also found that the oligopeptidase B-2 gene is expressed in all cycle stages of L. amazonensis. A phylogenetic analysis indicated that oligopeptidase B-2 is a new member of oligopeptidase B.
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