The Plasmodium vivax rhoptry-associated protein 1

Oscar Perez-Leal; Alvaro Mongui; Jimena Cortes; Gloria Yepes; Jesus Leiton; Manuel A. Patarroyo

doi:10.1016/j.bbrc.2006.01.061

The Plasmodium vivax rhoptry-associated protein 1

Título traducido de la contribución: La proteína 1 asociada al salto de Plasmodium vivax

Oscar Perez-Leal
, Alvaro Mongui
, Jimena Cortes
, Gloria Yepes
, Jesus Leiton
, Manuel A. Patarroyo

Producción científica: Contribución a revista › Artículo de Investigación › revisión exhaustiva

20 Citas (Scopus)

Resumen

Los rhoptries son orgánulos celulares localizados en el polo apical de los parásitos apicomplexanos. Su contenido es rico en lípidos y proteínas que se liberan durante la invasión de la célula diana. La proteína 1 asociada a rhoptry (RAP1) de Plasmodium falciparum ha sido la más estudiada entre las proteínas rhoptry de esta especie de parásito y se considera un buen candidato para la vacuna antipalúdica, ya que muestra poco polimorfismo e induce anticuerpos en humanos infectados. Los anticuerpos monoclonales dirigidos contra RAP1 también son capaces de inhibir la invasión de células diana in vitro y se induce protección contra la provocación experimental con P. falciparum cuando se inmuniza a primates no humanos con esta proteína expresada en su forma recombinante. Este estudio describe la identificación y caracterización de RAP1 en Plasmodium vivax, la especie de parásito causante de malaria más extendida en humanos, que produce más de 80 millones de infecciones anuales, principalmente en Asia y Latinoamérica. Esta nueva proteína está codificada por un gen de dos exones, se procesa proteolíticamente de forma similar a su homóloga falciparum y, según lo observado por microscopía, el patrón de inmunofluorescencia mostrado es sugestivo de su localización en la rampa. Deberían llevarse a cabo nuevos estudios para evaluar la eficacia protectora del RAP1 de P. vivax en primates no humanos, teniendo en cuenta la importancia de su homólogo de P. falciparum como candidato a vacuna antipalúdica.

Título traducido de la contribución	La proteína 1 asociada al salto de Plasmodium vivax
Idioma original	Inglés estadounidense
Páginas (desde-hasta)	1053-1058
Número de páginas	6
Publicación	Biochemical and Biophysical Research Communications
Volumen	341
N.º	4
DOI	https://doi.org/10.1016/j.bbrc.2006.01.061
Estado	Publicada - mar 24 2006
Publicado de forma externa	Sí

ODS de las Naciones Unidas

Este resultado contribuye a los siguientes Objetivos de Desarrollo Sostenible

ODS 3: Salud y bienestar

Áreas temáticas de ASJC Scopus

Biología molecular

Acceder al documento

10.1016/j.bbrc.2006.01.061

Citar esto

@article{18fe027a8f464cf289b3c946c3c9bbd6,

title = "The Plasmodium vivax rhoptry-associated protein 1",

abstract = "Rhoptries are cellular organelles localized at the apical pole of apicomplexan parasites. Their content is rich in lipids and proteins that are released during target cell invasion. Plasmodium falciparum rhoptry-associated protein 1 (RAP1) has been the most widely studied among this parasite species' rhoptry proteins and is considered to be a good anti-malarial vaccine candidate since it displays little polymorphism and induces antibodies in infected humans. Monoclonal antibodies directed against RAP1 are also able to inhibit target cell invasion in vitro and protection against P. falciparum experimental challenge is induced when non-human primates are immunized with this protein expressed in its recombinant form. This study describes identifying and characterizing RAP1 in Plasmodium vivax, the most widespread parasite species causing malaria in humans, producing more than 80 million infections yearly, mainly in Asia and Latin America. This new protein is encoded by a two-exon gene, is proteolytically processed in a similar manner to its falciparum homologue and, as observed by microscopy, the immunofluorescence pattern displayed is suggestive of its rhoptry localization. Further studies evaluating P. vivax RAP1 protective efficacy in non-human primates should be carried out taking into account the relevance that its P. falciparum homologue has as an anti-malarial vaccine candidate. {\textcopyright} 2006 Elsevier Inc. All rights reserved.",

author = "Oscar Perez-Leal and Alvaro Mongui and Jimena Cortes and Gloria Yepes and Jesus Leiton and Patarroyo, \{Manuel A.\}",

year = "2006",

month = mar,

day = "24",

doi = "10.1016/j.bbrc.2006.01.061",

language = "English (US)",

volume = "341",

pages = "1053--1058",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier BV",

number = "4",

}

TY - JOUR

T1 - The Plasmodium vivax rhoptry-associated protein 1

AU - Perez-Leal, Oscar

AU - Mongui, Alvaro

AU - Cortes, Jimena

AU - Yepes, Gloria

AU - Leiton, Jesus

AU - Patarroyo, Manuel A.

PY - 2006/3/24

Y1 - 2006/3/24

N2 - Rhoptries are cellular organelles localized at the apical pole of apicomplexan parasites. Their content is rich in lipids and proteins that are released during target cell invasion. Plasmodium falciparum rhoptry-associated protein 1 (RAP1) has been the most widely studied among this parasite species' rhoptry proteins and is considered to be a good anti-malarial vaccine candidate since it displays little polymorphism and induces antibodies in infected humans. Monoclonal antibodies directed against RAP1 are also able to inhibit target cell invasion in vitro and protection against P. falciparum experimental challenge is induced when non-human primates are immunized with this protein expressed in its recombinant form. This study describes identifying and characterizing RAP1 in Plasmodium vivax, the most widespread parasite species causing malaria in humans, producing more than 80 million infections yearly, mainly in Asia and Latin America. This new protein is encoded by a two-exon gene, is proteolytically processed in a similar manner to its falciparum homologue and, as observed by microscopy, the immunofluorescence pattern displayed is suggestive of its rhoptry localization. Further studies evaluating P. vivax RAP1 protective efficacy in non-human primates should be carried out taking into account the relevance that its P. falciparum homologue has as an anti-malarial vaccine candidate. © 2006 Elsevier Inc. All rights reserved.

AB - Rhoptries are cellular organelles localized at the apical pole of apicomplexan parasites. Their content is rich in lipids and proteins that are released during target cell invasion. Plasmodium falciparum rhoptry-associated protein 1 (RAP1) has been the most widely studied among this parasite species' rhoptry proteins and is considered to be a good anti-malarial vaccine candidate since it displays little polymorphism and induces antibodies in infected humans. Monoclonal antibodies directed against RAP1 are also able to inhibit target cell invasion in vitro and protection against P. falciparum experimental challenge is induced when non-human primates are immunized with this protein expressed in its recombinant form. This study describes identifying and characterizing RAP1 in Plasmodium vivax, the most widespread parasite species causing malaria in humans, producing more than 80 million infections yearly, mainly in Asia and Latin America. This new protein is encoded by a two-exon gene, is proteolytically processed in a similar manner to its falciparum homologue and, as observed by microscopy, the immunofluorescence pattern displayed is suggestive of its rhoptry localization. Further studies evaluating P. vivax RAP1 protective efficacy in non-human primates should be carried out taking into account the relevance that its P. falciparum homologue has as an anti-malarial vaccine candidate. © 2006 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.bbrc.2006.01.061

DO - 10.1016/j.bbrc.2006.01.061

M3 - Research Article

C2 - 16458855

SN - 0006-291X

VL - 341

SP - 1053

EP - 1058

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

The Plasmodium vivax rhoptry-associated protein 1

Resumen

ODS de las Naciones Unidas

Áreas temáticas de ASJC Scopus

Acceder al documento

Huella

Citar esto