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Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

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Expression and substrate specificity of a recombinant cysteine proteinase B of Leishmania braziliensis

Lanfranco, Maria F. and Loayza-Muro, Raul and Clark, Daniel and Nunez, Regina and Zavaleta, Amparo I. and Jimenez, Maribel and Meidal, Morten and Coombs, G.H. and Mottram, J.C. and Izidoro, Mario and Juliano, Maria A. and Juliano, Luiz and Arevalo, Jorge (2008) Expression and substrate specificity of a recombinant cysteine proteinase B of Leishmania braziliensis. Molecular and Biochemical Parasitology, 161 (2). pp. 91-100. ISSN 0166-6851

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Abstract

The cysteine proteinase B of Leishmania parasites is an important virulence factor. In this study we have expressed, isolated and characterized for the first time a recombinant CPB from Leishmania braziliensis, the causative agent of mucocutaneous leishmaniosis. The mature region of the recombinant CPB shares a high percentage identity with its Leishmania mexicana CPB2.8 (rCPB2.8-CTE) counterpart (76.36%) and has identical amino acid residues at the S1, catalytic triad and S′1 subsites. Nevertheless, when the kinetics of substrate hydrolysis was measured using a combinatorial library of internally quenched fluorescent peptides based upon the lead sequence Abz-KLRSSKQ-EDDnp, significant differences were obtained. These results suggest that the differences in substrate utilization observed between the L. mexicana and L. braziliensis CPs must be related to amino acid modifications outside the core of the active site cleft. Moreover, a potent inhibitor with Pro at P1 and high affinity for L. braziliensis recombinant CPB showed less affinity to L. mexicana CPB 2.8, which preferred Phe, Leu, and Asn at the same position.