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 (...

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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)
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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
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rights_invalid_str_mv Abierto (Texto Completo)
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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
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