f Multiple high activity cysteine proteases of Leishmania mexicana are encoded by the Imcpb gene array
- Authors: Colin D. Robertson†, Graham H. Coombs
- Author for correspondence: Colin D. Robertson. Tel: +44 41 339 8855. Fax: +44 41 330 5603.
- Microbiology, February 1994 140: 417-424, doi: 10.1099/13500872-140-2-417
- Subject: Biochemistry
- Published Online:
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.
Present address: Department of Veterinary Parasitology, University of Glasgow, Glasgow G61 1RQ, UK.
© Society For General Microbiology 1994 | Published by the Microbiology Society
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