Babesia bigemina: Identification of B cell epitopes associated with parasitized erythrocytes

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dc.contributor.authorVidotto, Odilon
dc.contributor.authorMcElwain, Terry F.
dc.contributor.authorMachado, Rosangela Z. [UNESP]
dc.contributor.authorPerryman, Lance E.
dc.contributor.authorSuarez, Carlos E.
dc.contributor.authorPalmer, Guy H.
dc.contributor.institutionWashington State University
dc.contributor.institutionCCA-UEL
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionNorth Carolina State University
dc.date.accessioned2022-04-29T08:46:53Z
dc.date.available2022-04-29T08:46:53Z
dc.date.issued1995-01-01
dc.description.abstractRhoptries are involved in host cell invasion and rhoptry polypeptides, including the Babesia bigemina rhoptry-associated protein-1 (RAP-1), are targets for protective immune responses. Polyclonal antisera produced against isolated rhoptries is directed predominantly against RAP-1 and reacts with both the merozoite and the membrane of parasitized erythrocytes. To determine whether these B cell epitopes associated with the parasitized erythrocyte are derived from RAP-1 or, alternatively, from previously undetected merozoite polypeptides, monoclonal antibodies (mAbs) were generated from mice immunized with rhoptries isolated from the JG-29 clone of the Mexico strain. The anti-RAP-1 mAbs bound only merozoites in a punctate immunofluorescence pattern. A second group of four mAbs, none of which were reactive with RAP-1, bound the parasitized erythrocyte. Two of these latter mAbs, 64/44.17.3 and 64/05.7.2, reacted only with parasitized erythrocytes that had been permeabilized. MAb 64/44.17.3 bound a 54-kDa merozoite polypeptide while 64/05.7.2 bound a ≥225-kDa merozoite polypeptide. MAbs 64/32.8.5 and 64/38.5.3 recognized epitopes on 17.5- and 76-kDa polypeptides exposed on the external surface of intact parasitized erythrocytes. The results indicate that the identified RAP-1 epitopes are not associated with the erythrocyte cytoskeleton or membrane and that anti-RAP-1 immunity is most likely generated against the free merozoite. All new mAbs reacted with every B. bigemina strain tested (Mexico, Puerto Rico, St. Croix, Texcoco, Jaboticabal). The conservation of RAP-1 epitopes among these strains supports the continued testing of RAP-1 as a vaccine component. In addition, the identification of epitopes expressed on the surface of erythrocytes infected with all five strains provides new candidate immunogens. © 1995 Academic Press, Inc.en
dc.description.affiliationDepartment of Veterinary Microbiology Department of Pathology Washington State University, Pullman, WA, 99164-7040
dc.description.affiliationDepartment of Veterinary Preventive Medicine CCA-UEL, P.O. Box 6001, Londrina, Parana
dc.description.affiliationDepartment of Veterinary Pathobiology FCAVJ-UNESP, Jaboticabal, SP
dc.description.affiliationDepartment of Microbiology Pathology Parasitology North Carolina State University, Raleigh, NC
dc.description.affiliationUnespDepartment of Veterinary Pathobiology FCAVJ-UNESP, Jaboticabal, SP
dc.format.extent491-500
dc.identifierhttp://dx.doi.org/10.1006/expr.1995.1142
dc.identifier.citationExperimental Parasitology, v. 81, n. 4, p. 491-500, 1995.
dc.identifier.doi10.1006/expr.1995.1142
dc.identifier.issn0014-4894
dc.identifier.scopus2-s2.0-0029565718
dc.identifier.urihttp://hdl.handle.net/11449/231678
dc.language.isoeng
dc.relation.ispartofExperimental Parasitology
dc.sourceScopus
dc.titleBabesia bigemina: Identification of B cell epitopes associated with parasitized erythrocytesen
dc.typeArtigo

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