On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa)
The RBSA protein is encoded by a gene described in Plasmodium species having tropism for reticulocytes. Since this protein is antigenic in natural infections and can bind to target cells, it has been proposed as a potential candidate for an anti-Plasmodium vivax vaccine. However, genetic diversity (...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2018
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/19050
- Acceso en línea:
- http://repository.urosario.edu.co/handle/10336/19050
- Palabra clave:
- Blood Analysis
Chromatography
Dna Extraction
Escherichia Coli
Evolution
Gene Mutation
Genetic Polymorphism
Genetic Transformation
Genetic Variability
Human
Major Clinical Study
Microscopy
Plasmid
Plasmodium Vivax
Polymerase Chain Reaction
Reticulocyte
Sequence Analysis
Enfermedades
Article
Análisis de sangre
Cromatografía
ADN
- Rights
- License
- Abierto (Texto Completo)
id |
EDOCUR2_99a40d654a56a19aaee9520387475b3c |
---|---|
oai_identifier_str |
oai:repository.urosario.edu.co:10336/19050 |
network_acronym_str |
EDOCUR2 |
network_name_str |
Repositorio EdocUR - U. Rosario |
repository_id_str |
|
spelling |
520513f1-39d7-4a27-9a06-72226b1e0f2d60095c152d3-7555-4637-8c25-73f601f1e266600a933d343-0788-4635-9002-4943747140c3600fde509a6-b195-417e-a5b6-5a4aa4e8fbeb6007010ce6a-5c1d-4a8c-8e62-6cc183b4015e600796530656002019-02-12T19:57:27Z2019-02-12T19:57:27Z20182018The RBSA protein is encoded by a gene described in Plasmodium species having tropism for reticulocytes. Since this protein is antigenic in natural infections and can bind to target cells, it has been proposed as a potential candidate for an anti-Plasmodium vivax vaccine. However, genetic diversity (a challenge which must be overcome for ensuring fully effective vaccine design) has not been described at this locus. Likewise, the minimum regions mediating specific parasite-host interaction have not been determined. This is why the rbsa gene's evolutionary history is being here described, as well as the P. vivax rbsa (pvrbsa) genetic diversity and the specific regions mediating parasite adhesion to reticulocytes. Unlike what has previously been reported, rbsa was also present in several parasite species belonging to the monkey-malaria clade; paralogs were also found in Plasmodium parasites invading reticulocytes. The pvrbsa locus had less diversity than other merozoite surface proteins where natural selection and recombination were the main evolutionary forces involved in causing the observed polymorphism. The N-terminal end (PvRBSA-A) was conserved and under functional constraint; consequently, it was expressed as recombinant protein for binding assays. This protein fragment bound to reticulocytes whilst the C-terminus, included in recombinant PvRBSA-B (which was not under functional constraint), did not. Interestingly, two PvRBSA-A-derived peptides were able to inhibit protein binding to reticulocytes. Specific conserved and functionally important peptides within PvRBSA-A could thus be considered when designing a fully-effective vaccine against P. vivax. © 2018 Camargo-Ayala, Garzón-Ospina, Moreno-Pérez, Ricaurte-Contreras, Noya and Patarroyo.application/pdf10.3389/fgene.2018.003721664-8021http://repository.urosario.edu.co/handle/10336/19050engFrontiers in GeneticsVol. 9Frontiers in Genetics, ISSN:1664-8021, Vol. 9 (2018)https://www.frontiersin.org/articles/10.3389/fgene.2018.00372/fullAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2Abascal, F., Zardoya, R., Telford, M.J., TranslatorX: multiple alignment of nucleotide sequences guided by amino acid translations (2010) Nucleic Acids Res, 38 (WEB SERVER ISSUE), pp. W7-W13instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBlood AnalysisChromatographyDna ExtractionEscherichia ColiEvolutionGene MutationGenetic PolymorphismGenetic TransformationGenetic VariabilityHumanMajor Clinical StudyMicroscopyPlasmidPlasmodium VivaxPolymerase Chain ReactionReticulocyteSequence AnalysisEnfermedades616600ArticleAnálisis de sangreCromatografíaADNOn the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa)articleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Camargo-Ayala, Paola AndreaGarzón-Ospina, DiegoMoreno Pérez, Darwin AndrésRicaurte-Contreras, Laura AlejandraNoya, OscarPatarroyo, Manuel A.Camargo-Ayala, Paola AndreaGarzón-Ospina, DiegoMoreno Pérez, Darwin AndrésRicaurte-Contreras, Laura AlejandraNoya, OscarPatarroyo, Manuel A.ORIGINAL14.pdfapplication/pdf1629093https://repository.urosario.edu.co/bitstreams/da5615c0-34a3-4a6b-a352-03224ebf6b37/download459d214b19054677d0b95d81083ccbdcMD51TEXT14.pdf.txt14.pdf.txtExtracted texttext/plain89168https://repository.urosario.edu.co/bitstreams/c3f09ddf-096f-4b25-bccf-30fae5f01c29/download2c72c3e47b263858e5b2d1040250f257MD52THUMBNAIL14.pdf.jpg14.pdf.jpgGenerated Thumbnailimage/jpeg4226https://repository.urosario.edu.co/bitstreams/cc39dfc8-a396-4a87-a27a-a3ef25f87c96/downloadf41c97978dcde3eb97d4ca2ffe9074a6MD5310336/19050oai:repository.urosario.edu.co:10336/190502019-09-19 07:37:54.609585https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
title |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
spellingShingle |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) Blood Analysis Chromatography Dna Extraction Escherichia Coli Evolution Gene Mutation Genetic Polymorphism Genetic Transformation Genetic Variability Human Major Clinical Study Microscopy Plasmid Plasmodium Vivax Polymerase Chain Reaction Reticulocyte Sequence Analysis Enfermedades Article Análisis de sangre Cromatografía ADN |
title_short |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
title_full |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
title_fullStr |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
title_full_unstemmed |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
title_sort |
On the evolution and function of Plasmodium vivax reticulocyte binding surface antigen (pvrbsa) |
dc.subject.spa.fl_str_mv |
Blood Analysis Chromatography Dna Extraction Escherichia Coli Evolution Gene Mutation Genetic Polymorphism Genetic Transformation Genetic Variability Human Major Clinical Study Microscopy Plasmid Plasmodium Vivax Polymerase Chain Reaction Reticulocyte Sequence Analysis |
topic |
Blood Analysis Chromatography Dna Extraction Escherichia Coli Evolution Gene Mutation Genetic Polymorphism Genetic Transformation Genetic Variability Human Major Clinical Study Microscopy Plasmid Plasmodium Vivax Polymerase Chain Reaction Reticulocyte Sequence Analysis Enfermedades Article Análisis de sangre Cromatografía ADN |
dc.subject.ddc.spa.fl_str_mv |
Enfermedades |
dc.subject.keyword.spa.fl_str_mv |
Article |
dc.subject.lemb.spa.fl_str_mv |
Análisis de sangre Cromatografía ADN |
description |
The RBSA protein is encoded by a gene described in Plasmodium species having tropism for reticulocytes. Since this protein is antigenic in natural infections and can bind to target cells, it has been proposed as a potential candidate for an anti-Plasmodium vivax vaccine. However, genetic diversity (a challenge which must be overcome for ensuring fully effective vaccine design) has not been described at this locus. Likewise, the minimum regions mediating specific parasite-host interaction have not been determined. This is why the rbsa gene's evolutionary history is being here described, as well as the P. vivax rbsa (pvrbsa) genetic diversity and the specific regions mediating parasite adhesion to reticulocytes. Unlike what has previously been reported, rbsa was also present in several parasite species belonging to the monkey-malaria clade; paralogs were also found in Plasmodium parasites invading reticulocytes. The pvrbsa locus had less diversity than other merozoite surface proteins where natural selection and recombination were the main evolutionary forces involved in causing the observed polymorphism. The N-terminal end (PvRBSA-A) was conserved and under functional constraint; consequently, it was expressed as recombinant protein for binding assays. This protein fragment bound to reticulocytes whilst the C-terminus, included in recombinant PvRBSA-B (which was not under functional constraint), did not. Interestingly, two PvRBSA-A-derived peptides were able to inhibit protein binding to reticulocytes. Specific conserved and functionally important peptides within PvRBSA-A could thus be considered when designing a fully-effective vaccine against P. vivax. © 2018 Camargo-Ayala, Garzón-Ospina, Moreno-Pérez, Ricaurte-Contreras, Noya and Patarroyo. |
publishDate |
2018 |
dc.date.created.none.fl_str_mv |
2018 |
dc.date.issued.none.fl_str_mv |
2018 |
dc.date.accessioned.none.fl_str_mv |
2019-02-12T19:57:27Z |
dc.date.available.none.fl_str_mv |
2019-02-12T19:57:27Z |
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 |
10.3389/fgene.2018.00372 |
dc.identifier.issn.none.fl_str_mv |
1664-8021 |
dc.identifier.uri.none.fl_str_mv |
http://repository.urosario.edu.co/handle/10336/19050 |
identifier_str_mv |
10.3389/fgene.2018.00372 1664-8021 |
url |
http://repository.urosario.edu.co/handle/10336/19050 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationTitle.none.fl_str_mv |
Frontiers in Genetics |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 9 |
dc.relation.ispartof.spa.fl_str_mv |
Frontiers in Genetics, ISSN:1664-8021, Vol. 9 (2018) |
dc.relation.uri.spa.fl_str_mv |
https://www.frontiersin.org/articles/10.3389/fgene.2018.00372/full |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.acceso.spa.fl_str_mv |
Abierto (Texto Completo) |
rights_invalid_str_mv |
Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
institution |
Universidad del Rosario |
dc.source.bibliographicCitation.spa.fl_str_mv |
Abascal, F., Zardoya, R., Telford, M.J., TranslatorX: multiple alignment of nucleotide sequences guided by amino acid translations (2010) Nucleic Acids Res, 38 (WEB SERVER ISSUE), pp. W7-W13 |
dc.source.instname.none.fl_str_mv |
instname:Universidad del Rosario |
dc.source.reponame.none.fl_str_mv |
reponame:Repositorio Institucional EdocUR |
bitstream.url.fl_str_mv |
https://repository.urosario.edu.co/bitstreams/da5615c0-34a3-4a6b-a352-03224ebf6b37/download https://repository.urosario.edu.co/bitstreams/c3f09ddf-096f-4b25-bccf-30fae5f01c29/download https://repository.urosario.edu.co/bitstreams/cc39dfc8-a396-4a87-a27a-a3ef25f87c96/download |
bitstream.checksum.fl_str_mv |
459d214b19054677d0b95d81083ccbdc 2c72c3e47b263858e5b2d1040250f257 f41c97978dcde3eb97d4ca2ffe9074a6 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositorio institucional EdocUR |
repository.mail.fl_str_mv |
edocur@urosario.edu.co |
_version_ |
1814167735404331008 |