ArticlePloS one2012
Erythrocyte Binding Activity Displayed by a Selective Group of Plasmodium vivax Tryptophan Rich Antigens Is Inhibited by Patients' Antibodies.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Plasmodium knowlesi tryptophan-rich antigen 40.1 binds human erythrocyte spectrin alpha.PLoS neglected tropical diseases · 2026Article
- Adaptive evolution ofbioRxiv : the preprint server for biology · 2025Article
- Majority of the erythrocyte binding proteins of the Pvfam "a" family ofFrontiers in cellular and infection microbiology · 2025Article
- Comparative transcriptomics reveal differential gene expression among Plasmodium vivax geographical isolates and implications on erythrocyte invasion mechanisms.PLoS neglected tropical diseases · 2024Article
- Band 3-mediatedFrontiers in cellular and infection microbiology · 2022Article
- Alternative Invasion Mechanisms and Host Immune Response toMicroorganisms · 2020Review
- An Erythrocyte Membrane-Associated Antigen, PvTRAg-26 ofFrontiers in public health · 2020Article
- High prevalence and extended deletions in Plasmodium falciparum hrp2/3 genomic loci in Ethiopia.PloS one · 2020Article
- Transcriptome profiling ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Plasmodium vivax Infections of Duffy-Negative Erythrocytes: Historically Undetected or a Recent Adaptation?Trends in parasitology · 2018Review
- Easy and fast method for expression and native extraction of Plasmodium vivax Duffy binding protein fragments.Malaria journal · 2018Article
- Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth.The Journal of biological chemistry · 2017Article
- Article
- Host-parasite interaction: multiple sites in the Plasmodium vivax tryptophan-rich antigen PvTRAg38 interact with the erythrocyte receptor band 3.FEBS letters · 2016Article
- Interaction of Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 with Band 3 on Human Erythrocyte Surface Facilitates Parasite Growth.The Journal of biological chemistry · 2015Article
- Immunoprofiling of the tryptophan-rich antigen family in Plasmodium vivax.Infection and immunity · 2015Article
- CD4+ T cell response correlates with naturally acquired antibodies against Plasmodium vivax tryptophan-rich antigens.Infection and immunity · 2015Article
- Recognition of Human Erythrocyte Receptors by the Tryptophan-Rich Antigens of Monkey Malaria Parasite Plasmodium knowlesi.PloS one · 2015Article
- Mosquito Akirin as a potential antigen for malaria control.Malaria journal · 2014Article
- Defining the erythrocyte binding domains of Plasmodium vivax tryptophan rich antigen 33.5.PloS one · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasmodium vivax is a very common but non-cultivable malaria parasite affecting large human population in tropical world. To develop therapeutic reagents for this malaria, the parasite molecules involved in host-parasite interaction need to be investigated as they form effective vaccine or drug targets. We have investigated here the erythrocyte binding activity of a group of 15 different Plasmodium vivax tryptophan rich antigens (PvTRAgs). Only six of them, named PvTRAg, PvTRAg38, PvTRAg33.5, PvTRAg35.2 PvTRAg69.4 and PvATRAg74, showed binding to host erythrocytes. That the PvTRAgs binding to host erythrocytes was specific was evident from the competitive inhibition and saturation kinetics results. The erythrocyte receptors for these six PvTRAgs were resistant to trypsin and neuraminidase. These receptors were also chymotrypsin resistant except the receptors for PvTRAg38 and PvATRAg74 which were partially sensitive to this enzyme. The cross-competition studies showed that the chymotrypsin resistant RBC receptor for each of these two proteins was different. Altogether, there seems to be three RBC receptors for these six PvTRAgs and each PvTRAg has two RBC receptors. Both RBC receptors for PvTRAg, PvTRAg69.4, PvTRAg33.5, and PvTRAg35.2 were common to all these four proteins. These four PvTRAgs also shared one of their RBC receptors with PvTRAg38 as well as with PvATRAg74. The erythrocyte binding activity of these six PvTRAgs was inhibited by the respective rabbit polyclonal antibodies as well as by the natural antibodies produced by the P. vivax exposed individuals. It is concluded that only selective few PvTRAgs show erythrocyte binding activity involving different receptor molecules which can be blocked by the natural antibodies. Further studies on these receptor and ligands may lead to the development of therapeutic reagents for P. vivax malaria.
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