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Title
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Prolyl oligopeptidase of **Trypanosoma brucei** hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice
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Author
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Abstract
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| 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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Language
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English
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Source (journal)
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Microbes and infection / Institut Pasteur [Paris] - Paris, 1999, currens
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Publication
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Paris
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Elsevier
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2010
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ISSN
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1286-4579
[print]
1769-714X
[online]
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DOI
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10.1016/J.MICINF.2010.02.007
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Volume/pages
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12
:6
(2010)
, p. 457-466
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ISI
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000279044800005
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Full text (Publisher's DOI)
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