Identification and characterization of the Plasmodium vivax thrombospondin-related apical merozoite protein

Alvaro Mongui, Diana I. Angel, Darwin A. Moreno-Perez, Silvana Villarreal-Gonzalez, Hannia Almonacid, Magnolia Vanegas, Manuel A. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

7 Citas (Scopus)

Resumen

Background. Malaria caused by Plasmodium vivax is a major public health problem worldwide that affects 70-80 million people in the Middle East, Asia, Western Pacific, South America and the Caribbean. Despite its epidemiological importance, few antigens from this parasite species have been characterized to date compared to Plasmodium falciparum, due in part to the difficulties of maintaining an in vitro culture of P. vivax. This study describes the identification of the P. falciparum thrombospondin-related apical merozoite protein homologue in P. vivax (PvTRAMP) and examines its potential to be further evaluated as vaccine candidate. Methods. The gene encoding PvTRAMP was identified through an extensive search of the databases hosting the genome sequence of P. vivax. Genes adjacent to pvtramp were identified in silico to determine the degree of similarity between the protein sequences encoded by equivalent chromosomic fragments in P. falciparum and Plasmodium knowlesi. The pvtramp gene was amplified from cDNA of P. vivax schizont stages, cloned and expressed in Escherichia coli. Anti-PvTRAMP antisera was obtained by inoculating rabbits with PvTRAMP B cell epitopes produced as synthetic peptides in order to assess its recognition in parasite lysates by Western blot and in intact parasites by indirect immunofluorescence. The recognition of recombinant PvTRAMP by sera from P. vivax-infected individuals living in endemic areas was also assessed by ELISA. Results. The PfTRAMP homologue in P. vivax, here denoted as PvTRAMP, is a 340-amino-acid long antigen encoded by a single exon that could have a potential role in cytoadherence, as indicated by the presence of a thrombospondin structural homology repeat (TSR) domain. According to its transcription and expression profile, PvTRAMP is initially located at the parasite's apical end and later on the parasite surface. Recombinant PvTRAMP is recognized by sera from infected patients, therefore, indicating that it is targeted by the immune system during a natural infection with P. vivax. Conclusions. The results of this work support conducting further studies with PvTRAMP to evaluate its immunogenicity and protection-inducing ability in the Aotus animal model. © 2010 Mongui et al; licensee BioMed Central Ltd.
Idioma originalEnglish (US)
PublicaciónMalaria Journal
DOI
EstadoPublished - oct 15 2010

Huella dactilar

Thrombospondins
Plasmodium vivax
Merozoites
Parasites
Plasmodium falciparum
Proteins
Plasmodium knowlesi
Vivax Malaria
Genes
Schizonts
B-Lymphocyte Epitopes
Antigens
Middle East
Far East
South America
Indirect Fluorescent Antibody Technique
Serum
Computer Simulation
Immune Sera
Exons

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Mongui, Alvaro ; Angel, Diana I. ; Moreno-Perez, Darwin A. ; Villarreal-Gonzalez, Silvana ; Almonacid, Hannia ; Vanegas, Magnolia ; Patarroyo, Manuel A. / Identification and characterization of the Plasmodium vivax thrombospondin-related apical merozoite protein. En: Malaria Journal. 2010.
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title = "Identification and characterization of the Plasmodium vivax thrombospondin-related apical merozoite protein",
abstract = "Background. Malaria caused by Plasmodium vivax is a major public health problem worldwide that affects 70-80 million people in the Middle East, Asia, Western Pacific, South America and the Caribbean. Despite its epidemiological importance, few antigens from this parasite species have been characterized to date compared to Plasmodium falciparum, due in part to the difficulties of maintaining an in vitro culture of P. vivax. This study describes the identification of the P. falciparum thrombospondin-related apical merozoite protein homologue in P. vivax (PvTRAMP) and examines its potential to be further evaluated as vaccine candidate. Methods. The gene encoding PvTRAMP was identified through an extensive search of the databases hosting the genome sequence of P. vivax. Genes adjacent to pvtramp were identified in silico to determine the degree of similarity between the protein sequences encoded by equivalent chromosomic fragments in P. falciparum and Plasmodium knowlesi. The pvtramp gene was amplified from cDNA of P. vivax schizont stages, cloned and expressed in Escherichia coli. Anti-PvTRAMP antisera was obtained by inoculating rabbits with PvTRAMP B cell epitopes produced as synthetic peptides in order to assess its recognition in parasite lysates by Western blot and in intact parasites by indirect immunofluorescence. The recognition of recombinant PvTRAMP by sera from P. vivax-infected individuals living in endemic areas was also assessed by ELISA. Results. The PfTRAMP homologue in P. vivax, here denoted as PvTRAMP, is a 340-amino-acid long antigen encoded by a single exon that could have a potential role in cytoadherence, as indicated by the presence of a thrombospondin structural homology repeat (TSR) domain. According to its transcription and expression profile, PvTRAMP is initially located at the parasite's apical end and later on the parasite surface. Recombinant PvTRAMP is recognized by sera from infected patients, therefore, indicating that it is targeted by the immune system during a natural infection with P. vivax. Conclusions. The results of this work support conducting further studies with PvTRAMP to evaluate its immunogenicity and protection-inducing ability in the Aotus animal model. {\circledC} 2010 Mongui et al; licensee BioMed Central Ltd.",
author = "Alvaro Mongui and Angel, {Diana I.} and Moreno-Perez, {Darwin A.} and Silvana Villarreal-Gonzalez and Hannia Almonacid and Magnolia Vanegas and Patarroyo, {Manuel A.}",
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Identification and characterization of the Plasmodium vivax thrombospondin-related apical merozoite protein. / Mongui, Alvaro; Angel, Diana I.; Moreno-Perez, Darwin A.; Villarreal-Gonzalez, Silvana; Almonacid, Hannia; Vanegas, Magnolia; Patarroyo, Manuel A.

En: Malaria Journal, 15.10.2010.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Identification and characterization of the Plasmodium vivax thrombospondin-related apical merozoite protein

AU - Mongui, Alvaro

AU - Angel, Diana I.

AU - Moreno-Perez, Darwin A.

AU - Villarreal-Gonzalez, Silvana

AU - Almonacid, Hannia

AU - Vanegas, Magnolia

AU - Patarroyo, Manuel A.

PY - 2010/10/15

Y1 - 2010/10/15

N2 - Background. Malaria caused by Plasmodium vivax is a major public health problem worldwide that affects 70-80 million people in the Middle East, Asia, Western Pacific, South America and the Caribbean. Despite its epidemiological importance, few antigens from this parasite species have been characterized to date compared to Plasmodium falciparum, due in part to the difficulties of maintaining an in vitro culture of P. vivax. This study describes the identification of the P. falciparum thrombospondin-related apical merozoite protein homologue in P. vivax (PvTRAMP) and examines its potential to be further evaluated as vaccine candidate. Methods. The gene encoding PvTRAMP was identified through an extensive search of the databases hosting the genome sequence of P. vivax. Genes adjacent to pvtramp were identified in silico to determine the degree of similarity between the protein sequences encoded by equivalent chromosomic fragments in P. falciparum and Plasmodium knowlesi. The pvtramp gene was amplified from cDNA of P. vivax schizont stages, cloned and expressed in Escherichia coli. Anti-PvTRAMP antisera was obtained by inoculating rabbits with PvTRAMP B cell epitopes produced as synthetic peptides in order to assess its recognition in parasite lysates by Western blot and in intact parasites by indirect immunofluorescence. The recognition of recombinant PvTRAMP by sera from P. vivax-infected individuals living in endemic areas was also assessed by ELISA. Results. The PfTRAMP homologue in P. vivax, here denoted as PvTRAMP, is a 340-amino-acid long antigen encoded by a single exon that could have a potential role in cytoadherence, as indicated by the presence of a thrombospondin structural homology repeat (TSR) domain. According to its transcription and expression profile, PvTRAMP is initially located at the parasite's apical end and later on the parasite surface. Recombinant PvTRAMP is recognized by sera from infected patients, therefore, indicating that it is targeted by the immune system during a natural infection with P. vivax. Conclusions. The results of this work support conducting further studies with PvTRAMP to evaluate its immunogenicity and protection-inducing ability in the Aotus animal model. © 2010 Mongui et al; licensee BioMed Central Ltd.

AB - Background. Malaria caused by Plasmodium vivax is a major public health problem worldwide that affects 70-80 million people in the Middle East, Asia, Western Pacific, South America and the Caribbean. Despite its epidemiological importance, few antigens from this parasite species have been characterized to date compared to Plasmodium falciparum, due in part to the difficulties of maintaining an in vitro culture of P. vivax. This study describes the identification of the P. falciparum thrombospondin-related apical merozoite protein homologue in P. vivax (PvTRAMP) and examines its potential to be further evaluated as vaccine candidate. Methods. The gene encoding PvTRAMP was identified through an extensive search of the databases hosting the genome sequence of P. vivax. Genes adjacent to pvtramp were identified in silico to determine the degree of similarity between the protein sequences encoded by equivalent chromosomic fragments in P. falciparum and Plasmodium knowlesi. The pvtramp gene was amplified from cDNA of P. vivax schizont stages, cloned and expressed in Escherichia coli. Anti-PvTRAMP antisera was obtained by inoculating rabbits with PvTRAMP B cell epitopes produced as synthetic peptides in order to assess its recognition in parasite lysates by Western blot and in intact parasites by indirect immunofluorescence. The recognition of recombinant PvTRAMP by sera from P. vivax-infected individuals living in endemic areas was also assessed by ELISA. Results. The PfTRAMP homologue in P. vivax, here denoted as PvTRAMP, is a 340-amino-acid long antigen encoded by a single exon that could have a potential role in cytoadherence, as indicated by the presence of a thrombospondin structural homology repeat (TSR) domain. According to its transcription and expression profile, PvTRAMP is initially located at the parasite's apical end and later on the parasite surface. Recombinant PvTRAMP is recognized by sera from infected patients, therefore, indicating that it is targeted by the immune system during a natural infection with P. vivax. Conclusions. The results of this work support conducting further studies with PvTRAMP to evaluate its immunogenicity and protection-inducing ability in the Aotus animal model. © 2010 Mongui et al; licensee BioMed Central Ltd.

U2 - 10.1186/1475-2875-9-283

DO - 10.1186/1475-2875-9-283

M3 - Article

JO - Malaria Journal

JF - Malaria Journal

SN - 1475-2875

ER -

Mongui A, Angel DI, Moreno-Perez DA, Villarreal-Gonzalez S, Almonacid H, Vanegas M y otros. Identification and characterization of the Plasmodium vivax thrombospondin-related apical merozoite protein. Malaria Journal. 2010 oct 15. https://doi.org/10.1186/1475-2875-9-283