ArticleMolecular microbiology2010
Functional diversification between two related Plasmodium falciparum merozoite invasion ligands is determined by changes in the cytoplasmic domain.
Article in Molecular microbiology, 2010. 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, 40 citations in OpenAlex.
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- Alternative Invasion Mechanisms and Host Immune Response toMicroorganisms · 2020Review
- Analysis of Plasmodium falciparum Rh2b deletion polymorphism across different transmission areas.Scientific reports · 2020Article
- Temporal changes in Plasmodium falciparum reticulocyte binding protein homolog 2b (PfRh2b) in Senegal and The Gambia.Malaria journal · 2019Article
- A pan-apicomplexan phosphoinositide-binding protein acts in malarial microneme exocytosis.EMBO reports · 2019Article
- A forward genetic screen reveals a primary role for Plasmodium falciparum Reticulocyte Binding Protein Homologue 2a and 2b in determining alternative erythrocyte invasion pathways.PLoS pathogens · 2018Article
- PfCDPK1 mediated signaling in erythrocytic stages of Plasmodium falciparum.Nature communications · 2017Article
- Merozoite surface proteins in red blood cell invasion, immunity and vaccines against malaria.FEMS microbiology reviews · 2016Review
- The Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion Proteins to Aldolase Is Enhanced by Phosphorylation.PloS one · 2016Article
- Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.PLoS pathogens · 2015Article
- Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans.Cell host & microbe · 2015Article
- Malaria invasion ligand RH5 and its prime candidacy in blood-stage malaria vaccine design.Human vaccines & immunotherapeutics · 2015Review
- Antibody response against three Plasmodium falciparum merozoite antigens in Mamuju District, West Sulawesi Province, Indonesia.Malaria journal · 2014Article
- Genome sequencing of chimpanzee malaria parasites reveals possible pathways of adaptation to human hosts.Nature communications · 2014Article
- Inside scoop on outside proteins.Infection and immunity · 2014Article
- Plasmodium falciparum merozoite surface antigen, PfRH5, elicits detectable levels of invasion-inhibiting antibodies in humans.The Journal of infectious diseases · 2013Article
- Specific phosphorylation of the PfRh2b invasion ligand of Plasmodium falciparum.The Biochemical journal · 2013Article
- Article
- Plasmodium falciparum merozoite invasion is inhibited by antibodies that target the PfRh2a and b binding domains.PLoS pathogens · 2011Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The pathogenesis of Plasmodium falciparum depends on efficient invasion into host erythrocytes. Parasite ligands encoded by multi-gene families interact with erythrocyte receptors. P. falciparum reticulocyte binding protein homologues (PfRhs) are expressed at the apical surface of invasive merozoites and have divergent ectodomains that are postulated to bind different erythrocyte receptors. Variant expression of these paralogues results in the use of alternative invasion pathways. Two PfRh proteins, PfRh2a and PfRh2b, are identical for 2700 N-terminal amino acids and differ only in a C-terminal 500 amino acid region, which includes a unique ectodomain, transmembrane domain and cytoplasmic domain. Despite their similarity, PfRh2b is required for a well-defined invasion pathway while PfRh2a is not required or sufficient for this pathway. Mapping the genomic region encoding these proteins revealed a recombinogenic locus with PfRh2a and PfRh2b in a head-to-head orientation. We have generated viable PfRh2a/2b chimeric parasites to identify the regions required for alternative invasion pathway utilization. We find that the differential ability to use these pathways is conferred by the cytoplasmic domains of PfRh2a and PfRh2b, not the ectodomain or transmembrane regions. Our results highlight the importance of the cytoplasmic domain for functional diversification of a major adhesive ligand family in malaria parasites.
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