Publication
Title
Prolyl oligopeptidase of **Trypanosoma brucei** hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice
Author
Abstract
Proteases playimportantrolesinmanybiologicalprocessesofparasites,includingtheirhostinteractions.Insleepingsickness, Trypanosoma brucei proteases releasedintothehostbloodstreamcouldhydrolyzehostfactors,suchashormones,contributingtothedevelopmentofthe diseasessymptoms.Inthisstudy,wepresenttheidentificationofthe T. brucei prolyl oligopeptidasegene( poptb) andthecharacterizationofits corresponding enzyme,POPTb.SecondarystructurepredictionsofPOPTbshowastructuralcompositionhighlysimilartootherPOPs. Recombinant POPTbproducedin E. coli was activeandhighlysensitivetoinhibitorsof Trypanosoma cruzi POP Tc80.Theseinhibitors,which prevent T. cruzi entry intonon-phagocyticcells,arrestedgrowthofthe T. brucei bloodstream forminadose-dependentmanner.POPTb hydrolyzes peptidehormonescontainingProorAlaattheP1positionataslightlyalkalinepH,andalsocleavestypeIcollagen in vitro and nativecollagenpresentinratmesentery.Furthermore,POPTbisreleasedintothebloodstreamof T. brucei infected micewhereitremains active.ThesedatasuggestthatPOPTbmightcontributetothepathogenesisofsleepingsickness.
Language
English
Source (journal)
Microbes and infection. - Paris, 1999, currens
Publication
Paris : 2010
ISSN
1286-4579
Volume/pages
12:6(2010), p. 457-466
ISI
000279044800005
Full text (Publisher's DOI)
UAntwerpen
Faculty/Department
Research group
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 14.09.2010
Last edited 21.06.2017
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