DESARROLLO DE LA TROPOMIOSINA A RECOMBINANTE ANTIGÉNICA de Echinococcus granulosus EN UN SISTEMA BACTERIANO COMO CANDIDATO VACUNAL CONTRA LA EQUINOCOCOSIS CANINA.

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Bibliographic Details
Title: DESARROLLO DE LA TROPOMIOSINA A RECOMBINANTE ANTIGÉNICA de Echinococcus granulosus EN UN SISTEMA BACTERIANO COMO CANDIDATO VACUNAL CONTRA LA EQUINOCOCOSIS CANINA.
Alternate Title: DEVELOPMENT OF THE ANTIGENIC RECOMBINANT TROPOMYOSIN OF Echinococcus granulosus IN A BACTERIAL SYSTEM AS A VACCINAL CANDIDATE AGAINST CANINE ECHINOCOCCOSIS.
Authors: Acosta-Benites, Janet jamnethe5@gmail.com, Jara, Luis M., Verastegui Pimentel, Manuela, Obregón Maldonado, Pepe M., Altamirano-Zevallos, Faride, Valencia Mamani, Nicasio, Gavidia, Cesar M.
Source: Revista Peruana de Medicina Experimental y Salud Pública. 2024, Vol. 41 Issue 4, p411-416. 6p.
Subjects: RECOMBINANT proteins, ECHINOCOCCUS granulosus, ESCHERICHIA coli, TWO-dimensional electrophoresis, GENETIC vectors
Abstract (English): This study aimed to clone, express and produce the recombinant Echinococcus granulosus tropomyosin isoform A protein (EgTrpA) that maintains its antigenic and immunogenic properties as a potential vaccine candidate for dogs and sheep. The Echinococcus granulosus tropomyosin protein (EgTrp) gene was cloned into two vectors: Tropo/His-tag [pET28a (+)] and Tropo/GST-tag (pGEX6P-1). It was then expressed in E. coli BL21. Protein identity was determined by two-dimensional electrophoresis. Immunogenicity and antigenicity were verified by immunizing rabbits with each recombinant protein and assessed by western blot and ELISA. Two-dimensional electrophoresis identified the recombinant EgTrp protein as isoform A. The recombinant proteins showed recognition reactions on Western Blot and serum from immunized rabbits showed an increase in Tropo/His-tag IgG antibodies similar to Tropo/GST-tag. The recombinant EgTrpA protein showed antigenic and immunogenic characteristics in laboratory animals. [ABSTRACT FROM AUTHOR]
Abstract (Spanish): El objetivo de este estudio fue clonar, expresar y producir la proteína recombinante tropomiosina isoforma A de Echinococcus granulosus (EgTrpA) que mantenga sus propiedades antigénicas e inmunogénicas como posible candidata a vacuna para perros y ovejas. El gen de la proteína tropomiosina de Echinococcus granulosus (EgTrp), se clono en dos vectores: Tropo/His-tag [pET28a (+)] y Tropo/GST-tag (pGEX6P-1). Luego, se expresó en E. coli BL21. La identidad de la proteína se determinó mediante electroforesis bidimensional. La inmunogenicidad y la antigenicidad se verificó mediante la inmunización de conejos con cada proteína recombinante y se evaluó mediante Western Blot y ELISA. La electroforesis bidimensional identificó la proteína recombinante EgTrp como isoforma A. Las proteínas recombinantes mostraron reacciones de reconocimiento en el Western Blot y el suero de los conejos inmunizados mostró un aumento de los anticuerpos IgG de Tropo/His-tag similar a Tropo/GST-tag. La proteína recombinante EgTrpA demostró características antigénicas e inmunogénicas en animales de laboratorio. [ABSTRACT FROM AUTHOR]
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Database: MedicLatina
Description
Abstract:This study aimed to clone, express and produce the recombinant Echinococcus granulosus tropomyosin isoform A protein (EgTrpA) that maintains its antigenic and immunogenic properties as a potential vaccine candidate for dogs and sheep. The Echinococcus granulosus tropomyosin protein (EgTrp) gene was cloned into two vectors: Tropo/His-tag [pET28a (+)] and Tropo/GST-tag (pGEX6P-1). It was then expressed in E. coli BL21. Protein identity was determined by two-dimensional electrophoresis. Immunogenicity and antigenicity were verified by immunizing rabbits with each recombinant protein and assessed by western blot and ELISA. Two-dimensional electrophoresis identified the recombinant EgTrp protein as isoform A. The recombinant proteins showed recognition reactions on Western Blot and serum from immunized rabbits showed an increase in Tropo/His-tag IgG antibodies similar to Tropo/GST-tag. The recombinant EgTrpA protein showed antigenic and immunogenic characteristics in laboratory animals. [ABSTRACT FROM AUTHOR]
ISSN:17264634
DOI:10.17843/rpmesp.2024.414.13854