ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structurally conserved erythrocyte-binding domain in Plasmodium provides a versatile scaffold for alternate receptor engagement.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 52 citations in OpenAlex.
- Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.The Biochemical journal · 2026Article
- Assessing the effect of parasite antigen genetic diversity on performance of Plasmodium vivax serological exposure markers for malaria: a multicentre observational diagnostic accuracy study.The Lancet. Microbe · 2026Observational
- Malian field isolates provide insight into Plasmodium malariae intra-erythrocytic development and invasion.PLoS neglected tropical diseases · 2025Article
- The reticulocyte restriction: invasion ligand RBP1a ofFrontiers in cellular and infection microbiology · 2025Article
- Functional and Immunologic Mapping of Domains of the Reticulocyte-Binding Protein Plasmodium vivax PvRBP2a.The Journal of infectious diseases · 2024Article
- Comparative transcriptomics reveal differential gene expression among Plasmodium vivax geographical isolates and implications on erythrocyte invasion mechanisms.PLoS neglected tropical diseases · 2024Article
- Evolution ofLe infezioni in medicina · 2023Review
- Cytonuclear coevolution in a holoparasitic plant with highly disparate organellar genomes.Plant molecular biology · 2022Article
- Genetic diversity of Plasmodium vivax reticulocyte binding protein 2b in global parasite populations.Parasites & vectors · 2022Article
- Geographical distribution and genetic diversity of Plasmodium vivax reticulocyte binding protein 1a correlates with patient antigenicity.PLoS neglected tropical diseases · 2022Article
- Comparison of total immunoglobulin G antibody responses to different protein fragments of Plasmodium vivax Reticulocyte binding protein 2b.Malaria journal · 2022Article
- Plasmodium simium: Population Genomics Reveals the Origin of a Reverse Zoonosis.The Journal of infectious diseases · 2021Article
- Plasmodium vivax binds host CD98hc (SLC3A2) to enter immature red blood cells.Nature microbiology · 2021Article
- Naturally acquired blocking human monoclonal antibodies to Plasmodium vivax reticulocyte binding protein 2b.Nature communications · 2021Article
- Progress towards the development of aExpert review of vaccines · 2021Review
- Alternative Invasion Mechanisms and Host Immune Response toMicroorganisms · 2020Review
- The RH5-CyRPA-Ripr Complex as a Malaria Vaccine Target.Trends in parasitology · 2020Review
- The Blood Stage Antigen RBP2-P1 of Plasmodium vivax Binds Reticulocytes and Is a Target of Naturally Acquired Immunity.Infection and immunity · 2020Article
- Plasmodium vivax Reticulocyte Binding Proteins for invasion into reticulocytes.Cellular microbiology · 2020Review
- Getting in: The structural biology of malaria invasion.PLoS pathogens · 2019Review
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Understanding how malaria parasites gain entry into human red blood cells is essential for developing strategies to stop blood stage infection. Plasmodium vivax preferentially invades reticulocytes, which are immature red blood cells. The organism has two erythrocyte-binding protein families: namely, the Duffy-binding protein (PvDBP) and the reticulocyte-binding protein (PvRBP) families. Several members of the PvRBP family bind reticulocytes, specifically suggesting a role in mediating host cell selectivity of P. vivax. Here, we present, to our knowledge, the first high-resolution crystal structure of an erythrocyte-binding domain from PvRBP2a, solved at 2.12 Å resolution. The monomeric molecule consists of 10 α-helices and one short β-hairpin, and, although the structural fold is similar to that of PfRh5--the essential invasion ligand in Plasmodium falciparum--its surface properties are distinct and provide a possible mechanism for recognition of alternate receptors. Sequence alignments of the crystallized fragment of PvRBP2a with other PvRBPs highlight the conserved placement of disulfide bonds. PvRBP2a binds mature red blood cells through recognition of an erythrocyte receptor that is neuraminidase- and chymotrypsin-resistant but trypsin-sensitive. By examining the patterns of sequence diversity within field isolates, we have identified and mapped polymorphic residues to the PvRBP2a structure. Using mutagenesis, we have also defined the critical residues required for erythrocyte binding. Characterization of the structural features that govern functional erythrocyte binding for the PvRBP family provides a framework for generating new tools that block P. vivax blood stage infection.
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