Characterizing PvARP, a novel Plasmodium vivax antigen

Darwin A. Moreno-Pérez, Ambar Saldarriaga, Manuel A. Patarroyo

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Background: Plasmodium vivax continues to be the most widely distributed malarial parasite species in tropical and sub-tropical areas, causing high morbidity indices around the world. Better understanding of the proteins used by the parasite during the invasion of red blood cells is required to obtain an effective vaccine against this disease. This study describes characterizing the P. vivax asparagine-rich protein (PvARP) and examines its antigenicity in natural infection. Methods. The target gene in the study was selected according to a previous in silico analysis using profile hidden Markov models which identified P. vivax proteins that play a possible role in invasion. Transcription of the arp gene in the P. vivax VCG-1 strain was here evaluated by RT-PCR. Specific human antibodies against PvARP were used to confirm protein expression by Western blot as well as its subcellular localization by immunofluorescence. Recognition of recombinant PvARP by sera from P. vivax-infected individuals was evaluated by ELISA. Results: VCG-1 strain PvARP is a 281-residue-long molecule, which is encoded by a single exon and has an N-terminal secretion signal, as well as a tandem repeat region. This protein is expressed in mature schizonts and is located on the surface of merozoites, having an apparent accumulation towards their apical pole. Sera from P. vivax-infected patients recognized the recombinant, thereby suggesting that this protein is targeted by the immune response during infection. Conclusions: This study showed the characterization of PvARP and its antigenicity. Further assays orientated towards evaluating this antigen's functional importance during parasite invasion are being carried out. © 2013 Moreno-Pérez et al.; licensee BioMed Central Ltd.
Original languageEnglish (US)
JournalMalaria Journal
DOIs
StatePublished - May 22 2013

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Plasmodium vivax
Asparagine
Antigens
Proteins
Parasites
Schizonts
Merozoites
Tandem Repeat Sequences
Infection
Computer Simulation
Genes
Fluorescent Antibody Technique
Blood Proteins
Exons
Vaccines
Erythrocytes
Western Blotting
Enzyme-Linked Immunosorbent Assay
Morbidity

Cite this

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title = "Characterizing PvARP, a novel Plasmodium vivax antigen",
abstract = "Background: Plasmodium vivax continues to be the most widely distributed malarial parasite species in tropical and sub-tropical areas, causing high morbidity indices around the world. Better understanding of the proteins used by the parasite during the invasion of red blood cells is required to obtain an effective vaccine against this disease. This study describes characterizing the P. vivax asparagine-rich protein (PvARP) and examines its antigenicity in natural infection. Methods. The target gene in the study was selected according to a previous in silico analysis using profile hidden Markov models which identified P. vivax proteins that play a possible role in invasion. Transcription of the arp gene in the P. vivax VCG-1 strain was here evaluated by RT-PCR. Specific human antibodies against PvARP were used to confirm protein expression by Western blot as well as its subcellular localization by immunofluorescence. Recognition of recombinant PvARP by sera from P. vivax-infected individuals was evaluated by ELISA. Results: VCG-1 strain PvARP is a 281-residue-long molecule, which is encoded by a single exon and has an N-terminal secretion signal, as well as a tandem repeat region. This protein is expressed in mature schizonts and is located on the surface of merozoites, having an apparent accumulation towards their apical pole. Sera from P. vivax-infected patients recognized the recombinant, thereby suggesting that this protein is targeted by the immune response during infection. Conclusions: This study showed the characterization of PvARP and its antigenicity. Further assays orientated towards evaluating this antigen's functional importance during parasite invasion are being carried out. {\circledC} 2013 Moreno-P{\'e}rez et al.; licensee BioMed Central Ltd.",
author = "Moreno-P{\'e}rez, {Darwin A.} and Ambar Saldarriaga and Patarroyo, {Manuel A.}",
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Characterizing PvARP, a novel Plasmodium vivax antigen. / Moreno-Pérez, Darwin A.; Saldarriaga, Ambar; Patarroyo, Manuel A.

In: Malaria Journal, 22.05.2013.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Characterizing PvARP, a novel Plasmodium vivax antigen

AU - Moreno-Pérez, Darwin A.

AU - Saldarriaga, Ambar

AU - Patarroyo, Manuel A.

PY - 2013/5/22

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N2 - Background: Plasmodium vivax continues to be the most widely distributed malarial parasite species in tropical and sub-tropical areas, causing high morbidity indices around the world. Better understanding of the proteins used by the parasite during the invasion of red blood cells is required to obtain an effective vaccine against this disease. This study describes characterizing the P. vivax asparagine-rich protein (PvARP) and examines its antigenicity in natural infection. Methods. The target gene in the study was selected according to a previous in silico analysis using profile hidden Markov models which identified P. vivax proteins that play a possible role in invasion. Transcription of the arp gene in the P. vivax VCG-1 strain was here evaluated by RT-PCR. Specific human antibodies against PvARP were used to confirm protein expression by Western blot as well as its subcellular localization by immunofluorescence. Recognition of recombinant PvARP by sera from P. vivax-infected individuals was evaluated by ELISA. Results: VCG-1 strain PvARP is a 281-residue-long molecule, which is encoded by a single exon and has an N-terminal secretion signal, as well as a tandem repeat region. This protein is expressed in mature schizonts and is located on the surface of merozoites, having an apparent accumulation towards their apical pole. Sera from P. vivax-infected patients recognized the recombinant, thereby suggesting that this protein is targeted by the immune response during infection. Conclusions: This study showed the characterization of PvARP and its antigenicity. Further assays orientated towards evaluating this antigen's functional importance during parasite invasion are being carried out. © 2013 Moreno-Pérez et al.; licensee BioMed Central Ltd.

AB - Background: Plasmodium vivax continues to be the most widely distributed malarial parasite species in tropical and sub-tropical areas, causing high morbidity indices around the world. Better understanding of the proteins used by the parasite during the invasion of red blood cells is required to obtain an effective vaccine against this disease. This study describes characterizing the P. vivax asparagine-rich protein (PvARP) and examines its antigenicity in natural infection. Methods. The target gene in the study was selected according to a previous in silico analysis using profile hidden Markov models which identified P. vivax proteins that play a possible role in invasion. Transcription of the arp gene in the P. vivax VCG-1 strain was here evaluated by RT-PCR. Specific human antibodies against PvARP were used to confirm protein expression by Western blot as well as its subcellular localization by immunofluorescence. Recognition of recombinant PvARP by sera from P. vivax-infected individuals was evaluated by ELISA. Results: VCG-1 strain PvARP is a 281-residue-long molecule, which is encoded by a single exon and has an N-terminal secretion signal, as well as a tandem repeat region. This protein is expressed in mature schizonts and is located on the surface of merozoites, having an apparent accumulation towards their apical pole. Sera from P. vivax-infected patients recognized the recombinant, thereby suggesting that this protein is targeted by the immune response during infection. Conclusions: This study showed the characterization of PvARP and its antigenicity. Further assays orientated towards evaluating this antigen's functional importance during parasite invasion are being carried out. © 2013 Moreno-Pérez et al.; licensee BioMed Central Ltd.

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