Title
Prolyl oligopeptidase of **Trypanosoma brucei** hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences. Pharmacy
Publication type
article
Publication
Paris ,
Subject
Human medicine
Source (journal)
Microbes and infection. - Paris, 1999, currens
Volume/pages
12(2010) :6 , p. 457-466
ISSN
1286-4579
ISI
000279044800005
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
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.
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