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Abstract
Babesia ovis, a tick-transmitted intraerythrocytic protozoan parasite, causes severe infections in small ruminants from Southern Europe, Middle East, and Northern Africa. With the aim of finding potential targets for the development of control methods against this parasite, sequence analysis of its genome led to the identification of four putative cysteine proteases of the C1A family. Orthology between B. ovis, B. bovis, T. annulata, and T. parva [ver mas...]
dc.contributor.authorCarletti, Tamara
dc.contributor.authorMesplet, Maria
dc.contributor.authorMira, Anabela
dc.contributor.authorWeir, William
dc.contributor.authorShiels, Brian
dc.contributor.authorGonzalez Oliva, Abel
dc.contributor.authorSchnittger, Leonhard
dc.contributor.authorFlorin-Christensen, Mónica
dc.contributor.authorBarreto, Carmo
dc.date.accessioned2017-09-13T14:48:02Z
dc.date.available2017-09-13T14:48:02Z
dc.date.issued2016
dc.identifier.issn1877-959X
dc.identifier.otherhttps://doi.org/10.1016/j.ttbdis.2015.09.002
dc.identifier.urihttp://hdl.handle.net/20.500.12123/1207
dc.identifier.urihttp://www.sciencedirect.com/science/article/pii/S1877959X1530008X
dc.description.abstractBabesia ovis, a tick-transmitted intraerythrocytic protozoan parasite, causes severe infections in small ruminants from Southern Europe, Middle East, and Northern Africa. With the aim of finding potential targets for the development of control methods against this parasite, sequence analysis of its genome led to the identification of four putative cysteine proteases of the C1A family. Orthology between B. ovis, B. bovis, T. annulata, and T. parva sequences showed that each B. ovis C1A peptidase sequence clustered within one of the four ortholog groups previously reported for these piroplasmids. The ortholog of bovipain-2 of B. bovis and falcipain-2 of Plasmodium falciparum, respectively, was designated “ovipain-2” and further characterized. In silico analysis showed that ovipain-2 has the typical topology of papain-like cysteine peptidases and a highly similar predicted three dimensional structure to bovipain-2 and falcipain-2, suggesting susceptibility to similar inhibitors. Immunoblotting using antibodies raised against a recombinant form of ovipain-2 (r-ovipain-2) demonstrated expression of ovipain-2 in in vitro cultured B. ovis merozoites. By immunofluorescence, these antibodies reacted with merozoites and stained the cytoplasm of infected erythrocytes. This suggests that ovipain-2 is secreted by the parasite and could be involved in intra- and extracellular digestion of hemoglobin and/or cleavage of erythrocyte proteins facilitating parasite egress. A significant reduction in the percentage of parasitized erythrocytes was obtained upon incubation of B. ovis in vitro cultures with anti-r-ovipain-2 antibodies, indicating an important functional role for ovipain-2 in the intra erythrocytic development cycle of this parasite. Finally, studies of the reactivity of sera from B. ovis-positive and negative sheep against r-ovipain-2 showed that this protease is expressed in vivo, and can be recognized by host antibodies. The results of this study suggest that ovipain-2 constitutes a potential target for immunotherapies and drug development against ovine babesiosis.eng
dc.formatapplication/pdfeng
dc.language.isoeng
dc.rightsinfo:eu-repo/semantics/restrictedAccesseng
dc.sourceTicks and tick-borne diseases 7 (1) : 85-93. (February 2016)
dc.subjectEnfermedades de los Animales
dc.subjectAnimal Diseaseseng
dc.subjectBabesia Ovis
dc.subjectPapaína
dc.subjectPapaineng
dc.subjectCisteína
dc.subjectCysteineeng
dc.titleCharacterization of a papain-like cysteine protease essential for the survival of Babesia ovis merozoiteseng
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/acceptedVersioneng
dc.description.origenInst. de Patobiología
dc.gic527
dc.description.filFil: Carletti, Tamara. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina
dc.description.filFil: Barreto, Carmo. Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica. Laboratório de Diagnóstico Biomolecular; Portugal. Universidade Nova de Lisboa. Instituto de Biologia Experimental e Tecnologica; Portugal
dc.description.filFil: Mesplet, Maria. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Cátedra de Enfermedades Infecciosas; Argentina
dc.description.filFil: Mira, Anabela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.filFil: Weir, William. Universityof Glasgow. College of Medical, Veterinary and Life Sciences; Reino Unido
dc.description.filFil: Shiels, Brian. Universityof Glasgow. College of Medical, Veterinary and Life Sciences; Reino Unido
dc.description.filFil: Gonzalez Oliva, Abel. Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica. Laboratório de Diagnóstico Biomolecular; Portugal. Universidade Nova de Lisboa. Instituto de Biologia Experimental e Tecnologica; Portugal
dc.description.filFil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiologia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.filFil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiologia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.subtypecientifico


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