ArticleInfection and immunity2013
The Plasmodium vivax merozoite surface protein 1 paralog is a novel erythrocyte-binding ligand of P. vivax.
Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 55 citations in OpenAlex.
- Anopheles ecology and serological evidence of malaria exposure in clinically malaria-free areas of Menoreh Hills Central Java, Indonesia.Scientific reports · 2026Article
- A novel micronemal protein MP38 is involved in the invasion of merozoites into erythrocytes.mBio · 2025Article
- Plasmodium vivax serological exposure markers: PvMSP1-42-induced humoral and memory B-cell response generates long-lived antibodies.PLoS pathogens · 2024Article
- A dot-blot ELISA preliminary evaluation using PvMSP1-42 recombinant protein as antigen for serological diagnosis of Plasmodium vivax infection in Thailand.European journal of microbiology & immunology · 2024Article
- Complement receptor 1 is the human erythrocyte receptor forProceedings of the National Academy of Sciences of the United States of America · 2024Article
- FT-GPI, a highly sensitive and accurate predictor of GPI-anchored proteins, reveals the composition and evolution of the GPI proteome in Plasmodium species.Malaria journal · 2023Article
- The direct binding ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Merozoite surface protein 1 paralog is involved in the human erythrocyte invasion of a zoonotic malaria,Frontiers in cellular and infection microbiology · 2023Article
- Review
- Zoonotic Malaria: Non-Pathogens (Basel, Switzerland) · 2021Review
- Two 20-Residue-Long Peptides Derived fromInternational journal of molecular sciences · 2021Article
- Alternative Invasion Mechanisms and Host Immune Response toMicroorganisms · 2020Review
- Cross-species reactivity of antibodies against Plasmodium vivax blood-stage antigens to Plasmodium knowlesi.PLoS neglected tropical diseases · 2020Article
- Low Levels of Polymorphisms and Negative Selection in Plasmodum knowlesi Merozoite Surface Protein 8 in Malaysian Isolates.The Korean journal of parasitology · 2019Article
- Identification and characterization of Pv50, a novel Plasmodium vivax merozoite surface protein.Parasites & vectors · 2019Article
- Inhibition of parasite invasion by monoclonal antibody against epidermal growth factor-like domain of Plasmodium vivax merozoite surface protein 1 paralog.Scientific reports · 2019Article
- Molecular and cellular interactions defining the tropism of Plasmodium vivax for reticulocytes.Current opinion in microbiology · 2018Review
- Erythrocyte-binding assays reveal higher binding of Plasmodium knowlesi Duffy binding protein to human FyParasites & vectors · 2018Article
- Plasmodium vivax Merozoite Surface Protein 1 Paralog as a Mediator of Parasite Adherence to Reticulocytes.Infection and immunity · 2018Article
- Immunological characterization of Plasmodium vivax Pv32, a novel predicted GPI-anchored merozoite surface protein.Malaria journal · 2018Article
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Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Merozoite surface protein 1 of Plasmodium vivax (PvMSP1), a glycosylphosphatidylinositol-anchored protein (GPI-AP), is a malaria vaccine candidate for P. vivax. The paralog of PvMSP1, named P. vivax merozoite surface protein 1 paralog (PvMSP1P; PlasmoDB PVX_099975), was recently identified and predicted as a GPI-AP. The similarities in genetic structural characteristics between PvMSP1 and PvMSP1P (e.g., size of open reading frames, two epidermal growth factor-like domains, and GPI anchor motif in the C terminus) led us to study this protein. In the present study, different regions of the PvMSP1P protein, demarcated based on the processed forms of PvMSP1, were expressed successfully as recombinant proteins [i.e., 83 (A, B, and C), 30, 38, 42, 33, and 19 fragments]. We studied the naturally acquired immune response against each fragment of recombinant PvMSP1P and the potential ability of each fragment to bind erythrocytes. The N-terminal fragment (83A) and two C-terminal fragments (33 and 19) reacted strongly with sera from P. vivax-infected patients, with 50 to 68% sensitivity and 95 to 96% specificity, respectively. Due to colocalization of PvMSP1P with PvMSP1, we supposed that PvMSP1P plays a similar role as PvMSP1 during erythrocyte invasion. An in vitro cytoadherence assay showed that PvMSP1P, especially the 19-kDa C-terminal region, could bind to erythrocytes. We also found that human sera from populations naturally exposed to vivax malaria and antisera obtained by immunization using the recombinant molecule PvMSP1P-19 inhibited in vitro binding of human erythrocytes to PvMSP1P-19. These results provide further evidence that the PvMSP1P might be an essential parasite adhesion molecule in the P. vivax merozoite and is a potential vaccine candidate against P. vivax.
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