The Plasmodium vivax rhoptry-associated protein 1

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...

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Autores:
Tipo de recurso:
Fecha de publicación:
2006
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/25944
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2006.01.061
https://repository.urosario.edu.co/handle/10336/25944
Palabra clave:
Malaria
Rhoptry
Plasmodium
RAP1
Vaccine candidate
Rights
License
Restringido (Acceso a grupos específicos)
id EDOCUR2_a0760cd7d14b6e72510dba03c2bb5e7b
oai_identifier_str oai:repository.urosario.edu.co:10336/25944
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling fd8d3f6a-56dc-44b0-b3d0-ccd34b8d828f-1914e954b-fc69-43d1-8b0b-ddda45ad991a-1bc380284-d23e-4afd-ad07-efa220c5bd4b-1474f6a28-e476-40f3-88c2-12caa0ed80e4-1b1a9fc9e-f3c2-4a42-9f4e-59db363b0583-179653065-12020-08-06T16:20:17Z2020-08-06T16:20:17Z2006-03-24Rhoptries 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.application/pdfhttps://doi.org/10.1016/j.bbrc.2006.01.061ISSN: 0006-291XEISSN: 1090-2104https://repository.urosario.edu.co/handle/10336/25944engElsevier1058No. 41053Biochemical and Biophysical Research CommunicationsVol. 341Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.341, No.4 (2006); pp.1053-1058https://www.sciencedirect.com/science/article/abs/pii/S0006291X06001434Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochemical and Biophysical Research Communicationsinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURMalariaRhoptryPlasmodiumRAP1Vaccine candidateThe Plasmodium vivax rhoptry-associated protein 1La proteína 1 asociada a la rhoptry de Plasmodium vivaxarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Perez-Leal, OscarMongui, AlvaroCortes, JimenaYepes, GloriaLeiton, JesusPatarroyo, Manuel A.10336/25944oai:repository.urosario.edu.co:10336/259442021-06-03 00:50:21.91https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv The Plasmodium vivax rhoptry-associated protein 1
dc.title.TranslatedTitle.spa.fl_str_mv La proteína 1 asociada a la rhoptry de Plasmodium vivax
title The Plasmodium vivax rhoptry-associated protein 1
spellingShingle The Plasmodium vivax rhoptry-associated protein 1
Malaria
Rhoptry
Plasmodium
RAP1
Vaccine candidate
title_short The Plasmodium vivax rhoptry-associated protein 1
title_full The Plasmodium vivax rhoptry-associated protein 1
title_fullStr The Plasmodium vivax rhoptry-associated protein 1
title_full_unstemmed The Plasmodium vivax rhoptry-associated protein 1
title_sort The Plasmodium vivax rhoptry-associated protein 1
dc.subject.keyword.spa.fl_str_mv Malaria
Rhoptry
Plasmodium
RAP1
Vaccine candidate
topic Malaria
Rhoptry
Plasmodium
RAP1
Vaccine candidate
description 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.
publishDate 2006
dc.date.created.spa.fl_str_mv 2006-03-24
dc.date.accessioned.none.fl_str_mv 2020-08-06T16:20:17Z
dc.date.available.none.fl_str_mv 2020-08-06T16:20:17Z
dc.type.eng.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1016/j.bbrc.2006.01.061
dc.identifier.issn.none.fl_str_mv ISSN: 0006-291X
EISSN: 1090-2104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/25944
url https://doi.org/10.1016/j.bbrc.2006.01.061
https://repository.urosario.edu.co/handle/10336/25944
identifier_str_mv ISSN: 0006-291X
EISSN: 1090-2104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 1058
dc.relation.citationIssue.none.fl_str_mv No. 4
dc.relation.citationStartPage.none.fl_str_mv 1053
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 341
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.341, No.4 (2006); pp.1053-1058
dc.relation.uri.spa.fl_str_mv https://www.sciencedirect.com/science/article/abs/pii/S0006291X06001434
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_16ec
dc.rights.acceso.spa.fl_str_mv Restringido (Acceso a grupos específicos)
rights_invalid_str_mv Restringido (Acceso a grupos específicos)
http://purl.org/coar/access_right/c_16ec
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Elsevier
dc.source.spa.fl_str_mv Biochemical and Biophysical Research Communications
institution Universidad del Rosario
dc.source.instname.none.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.none.fl_str_mv reponame:Repositorio Institucional EdocUR
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
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