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...
- 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)
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EDOCUR2 |
network_name_str |
Repositorio EdocUR - U. Rosario |
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|
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 |
_version_ |
1814167521990803456 |