%0 Journal Article %A Robertson, Colin D. %A Coombs, Graham H. %T Multiple high activity cysteine proteases of Leishmania mexicana are encoded by the Imcpb gene array %D 1994 %J Microbiology, %V 140 %N 2 %P 417-424 %@ 1465-2080 %R https://doi.org/10.1099/13500872-140-2-417 %K amino acid sequence %K cysteine proteases %K Imcpb genes %K Leishmania mexicana %I Microbiology Society, %X 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. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-140-2-417