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Multiple high activity cysteine proteases of Leishmania mexicana are encoded by the Imcpb gene array

Colin D. Robertson

Laboratory for Biochemical Parasitology, Department of Zoology, University of Glasgow, Glasgow G12 8QQ, UK

ABSTRACT

Summary: The interrelationship of the multiple cysteine proteases (CPs) found characteristically at high activity in Leishmania mexicana amastigotes has been investigated. The mature forms of the five enzymes of groups B and C, which have subtly different substrate preferences, are the same size. Enzymically deglycosylated group A CP proteins also have the same molecular mass. Proteases of all three groups are specifically recognized by antisera raised against the group B or group C CPs. In addition, CPs of groups A, B and C have highly similar N-terminal amino acid sequences. The consensus sequence matches that predicted from the sequenced Imcpb gene, which occurs in a tandem array of over ten similar genes. Thus, the results are consistent with the groups A, B and C CPs being products of different Imcpb genes within the array, the different genes encoding CPs with identical N-termini, but with limited amino acid substitutions within the mature enzyme accounting for the different properties of the CPs. Evidence is also presented to indicate membrane-association of proteolytically active but less processed forms of Imcpb products.

Author for correspondence: Colin D. Robertson. Tel: +44 41 339 8855. Fax: +44 41 330 5603.

Present address: Department of Veterinary Parasitology, University of Glasgow, Glasgow G61 1RQ, UK.

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