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Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes

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Moreno-Pérez, Darwin A.
Baquero, Luis A.
Chitiva-Ardila, Diana M.
Patarroyo, Manuel A.



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BioMed Central Ltd.

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Background: Plasmodium vivax uses multiple ligand-receptor interactions for preferential invasion of human reticulocytes. Several of these ligands have been identified by in silico approaches based on the role displayed by their orthologs in other Plasmodium species during initial adhesion or invasion. However, the cell adhesion role of proteins that are exclusive to species that specifically invade reticulocytes (as P. vivax and P. cynomolgi) has not been evaluated to date. This study aimed to characterise an antigen shared between Plasmodium species that preferentially infect reticulocytes with a focus on assessing its binding activity to target cells. Results: An in silico analysis was performed using P. vivax proteome data to identify and characterise one antigen shared between P. vivax and P. cynomolgi. This led to identification of the pvrbsa gene present in the P. vivax VCG-I strain genome. This gene is transcribed in mature schizonts and encodes a protein located on the parasite surface. rPvRBSA was antigenic and capable of binding to a population of reticulocytes with a different Duffy phenotype. Interestingly, the molecule showed a higher percentage of binding to immature human reticulocytes (CD71hi). Conclusions: This study describes for the first time, a molecule involved in host cell binding that is exclusive in reticulocyte-infecting Plasmodium species. This suggest that PvRBSA is an antigenic adhesin that plays a role in parasite binding to target cells. © 2017 The Author(s).
Palabras clave
Adhesin , Cd71 antigen , Duffy binding protein , Membrane antigen , Proteome , Reticulocyte binding surface antigen , Unclassified drug , Parasite antigen , Proteome , Protozoal protein , Antigen binding , Antigenicity , Article , Binding affinity , Cell interaction , Cell maturation , Cell population , Cell transport , Computer model , Controlled study , Gene , Gene identification , Genetic strain , Genetic transcription , Genome , Host cell , Host parasite interaction , Human , Human cell , Nonhuman , Nucleotide sequence , Phenotype , Plasmodium , Plasmodium cynomolgi , Plasmodium vivax , Prediction , Protein analysis , Protein localization , Proteomics , Rbsa gene , Reticulocyte , Schizont , Target cell , Cell adhesion , Erythrocyte , Genetics , Host pathogen interaction , Metabolism , Parasitology , Physiology , Plasmodium , Plasmodium vivax malaria , Reticulocyte , Antigens, protozoan , Cell adhesion , Erythrocytes , Genes, protozoan , Host-pathogen interactions , Humans , Malaria, vivax , Plasmodium , Plasmodium vivax , Proteome , Protozoan proteins , Reticulocytes , Adhesin , Antigenic protein , Plasmodium vivax , Reticulocyte
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