Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein

<p>Abstract</p> <p>Background</p> <p>Malaria caused by <it>Plasmodium vivax </it>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 epidemiologi...

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Main Authors: Villarreal-Gonzalez Silvana, Moreno-Perez Darwin A, Angel Diana I, Mongui Alvaro, Almonacid Hannia, Vanegas Magnolia, Patarroyo Manuel A
Format: Article
Language:English
Published: BMC 2010-10-01
Series:Malaria Journal
Online Access:http://www.malariajournal.com/content/9/1/283
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author Villarreal-Gonzalez Silvana
Moreno-Perez Darwin A
Angel Diana I
Mongui Alvaro
Almonacid Hannia
Vanegas Magnolia
Patarroyo Manuel A
author_facet Villarreal-Gonzalez Silvana
Moreno-Perez Darwin A
Angel Diana I
Mongui Alvaro
Almonacid Hannia
Vanegas Magnolia
Patarroyo Manuel A
author_sort Villarreal-Gonzalez Silvana
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>Malaria caused by <it>Plasmodium vivax </it>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 <it>Plasmodium falciparum</it>, due in part to the difficulties of maintaining an <it>in vitro </it>culture of <it>P. vivax</it>. This study describes the identification of the <it>P. falciparum </it>thrombospondin-related apical merozoite protein homologue in <it>P. vivax </it>(PvTRAMP) and examines its potential to be further evaluated as vaccine candidate.</p> <p>Methods</p> <p>The gene encoding PvTRAMP was identified through an extensive search of the databases hosting the genome sequence of <it>P. vivax</it>. Genes adjacent to <it>pvtramp </it>were identified <it>in silico </it>to determine the degree of similarity between the protein sequences encoded by equivalent chromosomic fragments in <it>P. falciparum </it>and <it>Plasmodium knowlesi</it>. The <it>pvtramp </it>gene was amplified from cDNA of <it>P. vivax </it>schizont stages, cloned and expressed in <it>Escherichia coli</it>. 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 <it>P. vivax-</it>infected individuals living in endemic areas was also assessed by ELISA.</p> <p>Results</p> <p>The PfTRAMP homologue in <it>P. vivax</it>, 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 <it>P. vivax.</it></p> <p>Conclusions</p> <p>The results of this work support conducting further studies with PvTRAMP to evaluate its immunogenicity and protection-inducing ability in the <it>Aotus </it>animal model.</p>
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spelling doaj.art-54bc597642b840ff94d6c7f956a98e692022-12-22T00:36:17ZengBMCMalaria Journal1475-28752010-10-019128310.1186/1475-2875-9-283Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite proteinVillarreal-Gonzalez SilvanaMoreno-Perez Darwin AAngel Diana IMongui AlvaroAlmonacid HanniaVanegas MagnoliaPatarroyo Manuel A<p>Abstract</p> <p>Background</p> <p>Malaria caused by <it>Plasmodium vivax </it>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 <it>Plasmodium falciparum</it>, due in part to the difficulties of maintaining an <it>in vitro </it>culture of <it>P. vivax</it>. This study describes the identification of the <it>P. falciparum </it>thrombospondin-related apical merozoite protein homologue in <it>P. vivax </it>(PvTRAMP) and examines its potential to be further evaluated as vaccine candidate.</p> <p>Methods</p> <p>The gene encoding PvTRAMP was identified through an extensive search of the databases hosting the genome sequence of <it>P. vivax</it>. Genes adjacent to <it>pvtramp </it>were identified <it>in silico </it>to determine the degree of similarity between the protein sequences encoded by equivalent chromosomic fragments in <it>P. falciparum </it>and <it>Plasmodium knowlesi</it>. The <it>pvtramp </it>gene was amplified from cDNA of <it>P. vivax </it>schizont stages, cloned and expressed in <it>Escherichia coli</it>. 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 <it>P. vivax-</it>infected individuals living in endemic areas was also assessed by ELISA.</p> <p>Results</p> <p>The PfTRAMP homologue in <it>P. vivax</it>, 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 <it>P. vivax.</it></p> <p>Conclusions</p> <p>The results of this work support conducting further studies with PvTRAMP to evaluate its immunogenicity and protection-inducing ability in the <it>Aotus </it>animal model.</p>http://www.malariajournal.com/content/9/1/283
spellingShingle Villarreal-Gonzalez Silvana
Moreno-Perez Darwin A
Angel Diana I
Mongui Alvaro
Almonacid Hannia
Vanegas Magnolia
Patarroyo Manuel A
Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein
Malaria Journal
title Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein
title_full Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein
title_fullStr Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein
title_full_unstemmed Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein
title_short Identification and characterization of the <it>Plasmodium vivax </it>thrombospondin-related apical merozoite protein
title_sort identification and characterization of the it plasmodium vivax it thrombospondin related apical merozoite protein
url http://www.malariajournal.com/content/9/1/283
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