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Ubiquity of Cysteine‐ and Metalloproteinase Activities in a Wide Range of Trypanosomatids
Author(s) -
BRANQUINHA MARTA H.,
VERMELHO ALANE B.,
GOLDENBERG SAMUEL,
BONALDO MYRNA C.
Publication year - 1996
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1996.tb04493.x
Subject(s) - biology , crithidia , metalloproteinase , cysteine , protozoa , biochemistry , leishmania , enzyme , trypanosoma , kinetoplastida , parasite hosting , microbiology and biotechnology , genetics , protozoal disease , malaria , immunology , world wide web , computer science
We have analysed the proteinase profiles of 11 species from 7 different genera of trypanosomatids by in situ detection of enzyme activities on SDS‐PAGE gels containing co‐polymerized gelatin as substrate, and the use of specific proteinase inhibitors. Our survey indicates that while cysteine‐ and metalloproteinases are distributed ubiquitously among trypanosomatids, there are marked differences between the enzyme profiles from the monogenetic ( Crithidia, Herpetomonas, Leptomonas ) and digenetic ( Trypanosoma, Endotrypanum, Phytomonas, Leishmania ) species. The detected metalloproteinase activities, ranging in size from 50–100 kDa, partitioned into the detergent‐phase after Triton X‐114 extraction, while most of cysteine proteinases, of three distinct molecular mass ranges (30–50 kDa, 80–100 kDa and 116–205 kDa), partitioned into the aqueous phase. Thus, within this group of organisms, the metalloproteinase activities seem to be predominantly membrane‐associated proteins. We also show that the plant parasites of the genus Phytomonas exhibit a distinctive cysteine proteinase profile that might be exploited further as a criterion for taxonomy of the genus.