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Microbiology 140 (1994), 417-424
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microbiology, Vol 140, 417-424, Copyright © 1994 by Society for General Microbiology

ARTICLES

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

CD Robertson and GH Coombs
Department of Zoology, University of Glasgow, UK.

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.


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Copyright © 1994 Society for General Microbiology.