ArticleMalaria journal2013
Characterizing PvARP, a novel Plasmodium vivax antigen.
Article in Malaria journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Using Plasmodium knowlesi as a model for screening Plasmodium vivax blood-stage malaria vaccine targets reveals new candidates.PLoS pathogens · 2021Article
- Self-assembling functional programmable protein array for studying protein-protein interactions in malaria parasites.Malaria journal · 2018Article
- Cross-species analysis of apical asparagine-rich protein of Plasmodium vivax and Plasmodium knowlesi.Scientific reports · 2018Article
- On the Evolution and Function ofFrontiers in genetics · 2018Article
- PvGAMA reticulocyte binding activity: predicting conserved functional regions by natural selection analysis.Parasites & vectors · 2017Article
- Characterising PvRBSA: an exclusive protein from Plasmodium species infecting reticulocytes.Parasites & vectors · 2017Article
- Asymptomatic Plasmodium vivax infections induce robust IgG responses to multiple blood-stage proteins in a low-transmission region of western Thailand.Malaria journal · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPlasmodium 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.
methodsThe 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.
resultsVCG-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.
conclusionsThis 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.
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