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Abstract
C1A cysteine peptidases have been shown to play an important role during apicomplexan invasion and egress of host red blood cells (RBCs) and therefore have been exploited as targets for drug development, in which peptidase specificity is deterministic. Babesia bovis genome is currently available and from the 17 putative cysteine peptidases annotated four belong to the C1A subfamily. In this study, we describe the biochemical characterization of a C1A [ver mas...]
dc.contributor.authorLu, Stephen
dc.contributor.authorAscencio, Mariano
dc.contributor.authorTorquato, Ricardo J.S.
dc.contributor.authorFlorin-Christensen, Mónica
dc.contributor.authorTanaka, Aparecida S.
dc.date.accessioned2022-01-14T11:46:50Z
dc.date.available2022-01-14T11:46:50Z
dc.date.issued2020-12
dc.identifier.issn0300-9084
dc.identifier.otherhttps://doi.org/10.1016/j.biochi.2020.09.012
dc.identifier.urihttp://hdl.handle.net/20.500.12123/11122
dc.identifier.urihttps://www.sciencedirect.com/science/article/abs/pii/S0300908420302182
dc.description.abstractC1A cysteine peptidases have been shown to play an important role during apicomplexan invasion and egress of host red blood cells (RBCs) and therefore have been exploited as targets for drug development, in which peptidase specificity is deterministic. Babesia bovis genome is currently available and from the 17 putative cysteine peptidases annotated four belong to the C1A subfamily. In this study, we describe the biochemical characterization of a C1A cysteine peptidase, named here BbCp (B. bovis cysteine peptidase) and evaluate its possible participation in the parasite asexual cycle in host RBCs. The recombinant protein was obtained in bacterial inclusion bodies and after a refolding process, presented typical kinetic features of the cysteine peptidase family, enhanced activity in the presence of a reducing agent, optimum pH between 6.5 and 7.0 and was inhibited by cystatins from R. microplus. Moreover, rBbCp substrate specificity evaluation using a peptide phage display library showed a preference for Val > Leu > Phe. Finally, antibodies anti-rBbCp were able to interfere with B. bovis growth in vitro, which highlights the BbCp as a potential target for drug design.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherElsevieres_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourceBiochimie 179 : 127-134 (December 2020)es_AR
dc.subjectCisteínaes_AR
dc.subjectCysteineeng
dc.subjectBabesia bovises_AR
dc.subjectPeptidasases_AR
dc.subjectPeptidaseseng
dc.subjectProteínas Recombinanteses_AR
dc.subjectRecombinant Proteinseng
dc.subjectAnticuerposes_AR
dc.subjectAntibodieseng
dc.titleKinetic characterization of a novel cysteine peptidase from the protozoan Babesia bovis, a potential target for drug designes_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/acceptedVersiones_AR
dc.description.origenInstituto de Patobiologíaes_AR
dc.description.filFil: Lu, Stephen. Universidade Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasiles_AR
dc.description.filFil: Ascencio, Mariano E. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentinaes_AR
dc.description.filFil: Torquato, Ricardo J.S. Universidade Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasiles_AR
dc.description.filFil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiologia; Argentinaes_AR
dc.description.filFil: Florin-Christensen, Monica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.es_AR
dc.description.filFil: Tanaka, Aparecida S. Universidade Federal de São Paulo. Escola Paulista de Medicina. Department of Biochemistry; Brasiles_AR
dc.description.filFil: Tanaka, Aparecida S. Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; Brasiles_AR
dc.subtypecientifico


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