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A proposed role for Leishmania major carboxypeptidase in peptide catabolism |
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| Authors: | Isaza Clara E Zhong Xuejun Rosas Lucia E White James D Chen Rita P-Y Liang George F-C Chan Sunney I Satoskar Abhay R Chan Michael K |
| Affiliation: | a The Ohio State Biophysics Program, The Ohio State University, Columbus, OH 43210, USA b Department of Chemistry, The Ohio State University, Columbus, OH 43210, USA c Department of Biochemistry, The Ohio State University, 484 West 12th Avenue, Room 776, Columbus, OH 43210, USA d Department of Microbiology, The Ohio State University, Columbus, OH 43210, USA e Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan f Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan |
| Abstract: | Leishmaniasis is a tropical disease caused by Leishmania, eukaryotic parasites transmitted to humans by sand flies. Towards the development of new chemotherapeutic targets for this disease, biochemical and in vivo expression studies were performed on one of two M32 carboxypeptidases present within the Leishmania major (LmaCP1) genome. Enzymatic studies reveal that like previously studied M32 carboxypeptidases, LmaCP1 cleaves substrates with a variety of C-terminal amino acids—the primary exception being those having C-terminal acidic residues. Cleavage assays with a series of FRET-based peptides suggest that LmaCP1 exhibits a substrate length restriction, preferring peptides shorter than 9-12 amino acids. The in vivo expression of LmaCP1 was analyzed for each major stage of the L. major life cycle. These studies reveal that LmaCP1 expression occurs only in procyclic promastigotes—the stage of life where the organism resides in the abdominal midgut of the insect. The implications of these results are discussed. |
| Keywords: | Leishmania M32 carboxypeptidase Stage-specific expression Metalloprotease |
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