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2030-01-01
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- IOC - Artigos de Periódicos [12120]
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BODO SP., A FREE-LIVING FLAGELLATE, EXPRESSES DIVERGENT PROTEOLYTIC ACTIVITIES FROM THE CLOSELY RELATED PARASITIC TRYPANOSOMATIDS
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Abstract
We report the characterization of cell-associated and extracellular peptidases of Bodo sp., a free-living flagellate of the
Bodonidae family, order Kinetoplastida, which is considered ancestral to the trypanosomatids. This bodonid isolate is phylogenetically
related to Bodo caudatus and Bodo curvifilus. The proteolytic activity profiles of Bodo sp. were determined by sodium dodecyl sulfatepolyacrylamide
gel electrophoresis containing co-polymerized gelatin, casein, hemoglobin, or bovine serum albumin as substrates. The
enzymatic complex degraded gelatin better in acidic pH, and under these conditions four proteolytic bands (120, 100, 90, and 75 kDa) were
detected in the cellular or extracellular extracts. Two peptidases (250 and 200 kDa) were exclusively detected with the substrate casein. All
these enzymes belong to the serine peptidase class, based on inhibition by aprotinin and phenylmethylsulfonyl fluoride. This is the first
biochemical characterization of peptidases in a free-living Bodo sp., potentially providing insight into the physiology of these protozoa and
the evolutionary importance of peptidases to the order Kinetoplastida as some of these enzymes are important virulence factors in pathogenic
trypanosomatids.
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