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Recombinant and native Tvi CATL from Trypanosoma vivax : Enzymatic characterisation and evaluation as a diagnostic target for animal African trypanosomosis

dc.rights.licenseopenen_US
dc.contributor.authorEYSSEN, Lauren E.-A.
dc.contributor.authorVATHER, Perina
dc.contributor.authorJACKSON, Laurelle
dc.contributor.authorXIMBA, Phindile
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorBITEAU, Nicolas
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorBALTZ, Théo
dc.contributor.authorBOULANGÉ, Alain
dc.contributor.authorBÜSCHER, Philippe
dc.contributor.authorCOETZER, Theresa H. T.
dc.date.accessioned2024-10-30T14:49:23Z
dc.date.available2024-10-30T14:49:23Z
dc.date.issued2018-07-01
dc.identifier.issn0166-6851en_US
dc.identifier.urioai:crossref.org:10.1016/j.molbiopara.2018.07.001
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/203006
dc.description.abstractEnAfrican animal trypanosomosis (nagana) is caused by tsetse-transmitted protozoan parasites. Their cysteine proteases are potential chemotherapeutic and diagnostic targets. The N-glycosylated catalytic domain of Trypanosoma vivax cathepsin L-like cysteine protease, rTviCATLcat, was recombinantly expressed and purified from culture supernatants while native TviCATL was purified from T. vivax Y486 parasite lysates. Typical of Clan CA, family C1 proteases, TviCATL activity is sensitive to E-64 and cystatin and substrate specificity is defined by the S2 pocket. Leucine was preferred in P2 and basic and non-bulky, hydrophobic residues accepted in P1 and P3 respectively. Reversible aldehyde inhibitors, antipain, chymostatin and leupeptin, with Arg in P1 and irreversible peptidyl chloromethylketone inhibitors with hydrophobic residues in P2 inhibited TviCATL activity. TviCATL digested host proteins: bovine haemoglobin, serum albumin, fibrinogen and denatured collagen (gelatine) over a wide pH range, including neutral to slightly acidic pH. The recombinant catalytic domain of TviCATL showed promise as a diagnostic target for detecting T. vivax infection in cattle in an indirect antibody detection ELISA.
dc.language.isoENen_US
dc.sourcecrossref
dc.subject.enCathepsin L-like peptidase; Diagnostic target; Nagana; Trypanosoma vivax; TviCATL.
dc.title.enRecombinant and native Tvi CATL from Trypanosoma vivax : Enzymatic characterisation and evaluation as a diagnostic target for animal African trypanosomosis
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.molbiopara.2018.07.001en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed29990512en_US
bordeaux.journalMolecular and Biochemical Parasitologyen_US
bordeaux.page50-54en_US
bordeaux.volume223en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcedissemin
hal.identifierhal-04760611
hal.version1
hal.date.transferred2024-10-30T14:49:26Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcedissemin
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Molecular%20and%20Biochemical%20Parasitology&rft.date=2018-07-01&rft.volume=223&rft.spage=50-54&rft.epage=50-54&rft.eissn=0166-6851&rft.issn=0166-6851&rft.au=EYSSEN,%20Lauren%20E.-A.&VATHER,%20Perina&JACKSON,%20Laurelle&XIMBA,%20Phindile&BITEAU,%20Nicolas&rft.genre=article


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