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Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes

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 invasi...

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Autores principales: Moreno-Pérez, Darwin A., Baquero, Luis A., Chitiva-Ardila, Diana M., Patarroyo, Manuel A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5437689/
https://www.ncbi.nlm.nih.gov/pubmed/28521840
http://dx.doi.org/10.1186/s13071-017-2185-6
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author Moreno-Pérez, Darwin A.
Baquero, Luis A.
Chitiva-Ardila, Diana M.
Patarroyo, Manuel A.
author_facet Moreno-Pérez, Darwin A.
Baquero, Luis A.
Chitiva-Ardila, Diana M.
Patarroyo, Manuel A.
author_sort Moreno-Pérez, Darwin A.
collection PubMed
description 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 (CD71(hi)). 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13071-017-2185-6) contains supplementary material, which is available to authorized users.
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spelling pubmed-54376892017-05-22 Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes Moreno-Pérez, Darwin A. Baquero, Luis A. Chitiva-Ardila, Diana M. Patarroyo, Manuel A. Parasit Vectors Research 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 (CD71(hi)). 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13071-017-2185-6) contains supplementary material, which is available to authorized users. BioMed Central 2017-05-18 /pmc/articles/PMC5437689/ /pubmed/28521840 http://dx.doi.org/10.1186/s13071-017-2185-6 Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Moreno-Pérez, Darwin A.
Baquero, Luis A.
Chitiva-Ardila, Diana M.
Patarroyo, Manuel A.
Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes
title Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes
title_full Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes
title_fullStr Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes
title_full_unstemmed Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes
title_short Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes
title_sort characterising pvrbsa: an exclusive protein from plasmodium species infecting reticulocytes
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5437689/
https://www.ncbi.nlm.nih.gov/pubmed/28521840
http://dx.doi.org/10.1186/s13071-017-2185-6
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