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

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorWashington State University-
Autor(es): dc.contributorCCA-UEL-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorNorth Carolina State University-
Autor(es): dc.creatorVidotto, Odilon-
Autor(es): dc.creatorMcElwain, Terry F.-
Autor(es): dc.creatorMachado, Rosangela Z.-
Autor(es): dc.creatorPerryman, Lance E.-
Autor(es): dc.creatorSuarez, Carlos E.-
Autor(es): dc.creatorPalmer, Guy H.-
Data de aceite: dc.date.accessioned2025-08-21T22:34:50Z-
Data de disponibilização: dc.date.available2025-08-21T22:34:50Z-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued1995-01-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1006/expr.1995.1142-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/231678-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/231678-
Descrição: dc.descriptionRhoptries 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.-
Descrição: dc.descriptionDepartment of Veterinary Microbiology Department of Pathology Washington State University, Pullman, WA, 99164-7040-
Descrição: dc.descriptionDepartment of Veterinary Preventive Medicine CCA-UEL, P.O. Box 6001, Londrina, Parana-
Descrição: dc.descriptionDepartment of Veterinary Pathobiology FCAVJ-UNESP, Jaboticabal, SP-
Descrição: dc.descriptionDepartment of Microbiology Pathology Parasitology North Carolina State University, Raleigh, NC-
Descrição: dc.descriptionDepartment of Veterinary Pathobiology FCAVJ-UNESP, Jaboticabal, SP-
Formato: dc.format491-500-
Idioma: dc.languageen-
Relação: dc.relationExperimental Parasitology-
???dc.source???: dc.sourceScopus-
Título: dc.titleBabesia bigemina: Identification of B cell epitopes associated with parasitized erythrocytes-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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