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Bodo sp., a Free-Living Flagellate, Expresses Divergent Proteolytic Activities from the Closely Related Parasitic Trypanosomatids

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 curvifi...

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Published in:The Journal of eukaryotic microbiology 2009-09, Vol.56 (5), p.454-458
Main Authors: D'AVILA-LEVY, CLAUDIA M, VOLOTÃO, ALINE C.C, ARAÚJO, FERNANDA M, DE JESUS, JOSÉ B, MOTTA, MARIA CRISTINA M, VERMELHO, ALANE B, SANTOS, ANDRÉ L.S, BRANQUINHA, MARTA H
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cited_by cdi_FETCH-LOGICAL-c4894-9a68dceecd0057b56080d2f14ed910c49bff251e3ec241018089b967f46bb9f33
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creator D'AVILA-LEVY, CLAUDIA M
VOLOTÃO, ALINE C.C
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SANTOS, ANDRÉ L.S
BRANQUINHA, MARTA H
description 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 sulfate-polyacrylamide 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.
doi_str_mv 10.1111/j.1550-7408.2009.00424.x
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subjects Animals
Aprotinin - pharmacology
Biological and medical sciences
Biological evolution
Bodo
Bodo caudatus
Bodonidae
Cluster Analysis
Cocos - parasitology
DNA, Protozoan - chemistry
DNA, Protozoan - genetics
DNA, Ribosomal - chemistry
DNA, Ribosomal - genetics
Electrophoresis, Polyacrylamide Gel - methods
Enzyme Inhibitors - pharmacology
evolution
Fundamental and applied biological sciences. Psychology
Genes, rRNA
Genetics of eukaryotes. Biological and molecular evolution
Kinetoplastida
Kinetoplastida - enzymology
Molecular Sequence Data
Molecular Weight
peptidase
Phenylmethylsulfonyl Fluoride - pharmacology
Phylogeny
Protozoa
Protozoan Proteins - analysis
Protozoan Proteins - chemistry
Protozoan Proteins - genetics
RNA, Protozoan - genetics
RNA, Ribosomal, 18S - genetics
Sequence Analysis, DNA
Serine Endopeptidases - analysis
Serine Endopeptidases - chemistry
Serine Endopeptidases - genetics
Systematics. Geographical distribution. Morphology. Cytology
Trypanosomatidae
title Bodo sp., a Free-Living Flagellate, Expresses Divergent Proteolytic Activities from the Closely Related Parasitic Trypanosomatids
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