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dc.contributor.authorGonzález Cerón, Lilia
dc.contributor.authorCebrián Carmona, José
dc.contributor.authorMesa Valle, Concepción
dc.contributor.authorGarcía Maroto, Federico
dc.contributor.authorSantillán Valenzuela, Frida
dc.contributor.authorGarrido Cárdenas, José Antonio
dc.date.accessioned2021-01-11T10:48:57Z
dc.date.available2021-01-11T10:48:57Z
dc.date.issued2020-12-28
dc.identifier.issn2073-4425
dc.identifier.urihttp://hdl.handle.net/10835/9270
dc.description.abstractPlasmodium vivax Cysteine-Rich Protective Antigen (CyRPA) is a merozoite protein participating in the parasite invasion of human reticulocytes. During natural P. vivax infection, antibody responses against PvCyRPA have been detected. In children, low anti-CyRPA antibody titers correlated with clinical protection, which suggests this protein as a potential vaccine candidate. This work analyzed the genetic and amino acid diversity of pvcyrpa in Mexican and global parasites. Consensus coding sequences of pvcyrpa were obtained from seven isolates. Other sequences were extracted from a repository. Maximum likelihood phylogenetic trees, genetic diversity parameters, linkage disequilibrium (LD), and neutrality tests were analyzed, and the potential amino acid polymorphism participation in B-cell epitopes was investigated. In 22 sequences from Southern Mexico, two synonymous and 21 nonsynonymous mutations defined nine private haplotypes. These parasites had the highest LD-R2 index and the lowest nucleotide diversity compared to isolates from South America or Asia. The nucleotide diversity and Tajima’s D values varied across the coding gene. The exon-1 sequence had greater diversity and Rm values than those of exon-2. Exon-1 had significant positive values for Tajima’s D, β-α values, and for the Z (HA: dN > dS) and MK tests. These patterns were similar for parasites of different origin. The polymorphic amino acid residues at PvCyRPA resembled the conformational B-cell peptides reported in PfCyRPA. Diversity at pvcyrpa exon-1 is caused by mutation and recombination. This seems to be maintained by balancing selection, likely due to selective immune pressure, all of which merit further study.es_ES
dc.language.isoenes_ES
dc.publisherMDPIes_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectPlasmodium vivaxes_ES
dc.subjectpvcyrpaes_ES
dc.subjectSouthern Mexicoes_ES
dc.subjectCysteine-Rich Protective Antigen (CyRPA)es_ES
dc.subjectmerozoite proteines_ES
dc.subjectgenetic diversityes_ES
dc.subjectTajima’s Des_ES
dc.subjectMK testes_ES
dc.subjectphylogenetic treees_ES
dc.subjectbalancing selectiones_ES
dc.titlePlasmodium vivax Cysteine-Rich Protective Antigen Polymorphism at Exon-1 Shows Recombination and Signatures of Balancing Selectiones_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttps://www.mdpi.com/2073-4425/12/1/29es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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