ArticleBiochimica et biophysica acta2014
Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3-MSP1 complex.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Host-pathogen interactions involved in erythrocyte invasion byFrontiers in cellular and infection microbiology · 2025Article
- Identification ofInfection and immunity · 2024Article
- Genetic polymorphism ofAccess microbiology · 2022Article
- Erythrocyte membrane proteins involved in the immune response to Plasmodium falciparum and Plasmodium vivax infection.Parasitology research · 2021Article
- Article
- Plasmodium falciparum Clag9-Associated PfRhopH Complex Is Involved in Merozoite Binding to Human Erythrocytes.Infection and immunity · 2020Article
- Human erythrocyte band 3 is a host receptor forBlood · 2019Article
- Anti-band 3 and anti-spectrin antibodies are increased in Plasmodium vivax infection and are associated with anemia.Scientific reports · 2018Article
- Plasmodium falciparum strains spontaneously switch invasion phenotype in suspension culture.Scientific reports · 2018Article
- Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum.Nature communications · 2017Article
- Article
- Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth.The Journal of biological chemistry · 2017Article
- Host-Parasite Interactions in Human Malaria: Clinical Implications of Basic Research.Frontiers in microbiology · 2017Review
- Red cell receptors as access points for malaria infection.Current opinion in hematology · 2016Review
- 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
- The influence of host genetics on erythrocytes and malaria infection: is there therapeutic potential?Malaria journal · 2015Review
- Host-parasite interactions that guide red blood cell invasion by malaria parasites.Current opinion in hematology · 2015Review
- Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Plasmodium falciparum takes advantage of two broadly defined alternate invasion pathways when infecting human erythrocytes: one that depends on and the other that is independent of host sialic acid residues on the erythrocyte surface. Within the sialic acid-dependent (SAD) and sialic acid-independent (SAID) invasion pathways, several alternate host receptors are used by P. falciparum based on its particular invasion phenotype. Earlier, we reported that two putative extracellular regions of human erythrocyte band 3 termed 5C and 6A function as host invasion receptor segments binding parasite proteins MSP1 and MSP9 via a SAID mechanism. In this study, we developed two mono-specific anti-peptide chicken IgY antibodies to demonstrate that the 5C and 6A regions of band 3 are exposed on the surface of human erythrocytes. These antibodies inhibited erythrocyte invasion by the P. falciparum 3D7 and 7G8 strains (SAID invasion phenotype), and the blocking effect was enhanced in sialic acid-depleted erythrocytes. In contrast, the IgY antibodies had only a marginal inhibitory effect on FCR3 and Dd2 strains (SAD invasion phenotype). A direct biochemical interaction between erythrocyte band 3 epitopes and parasite RhopH3, identified by the yeast two-hybrid screen, was established. RhopH3 formed a complex with MSP119 and the 5ABC region of band 3, and a recombinant segment of RhopH3 inhibited parasite invasion in human erythrocytes. Together, these findings provide evidence that erythrocyte band 3 functions as a major host invasion receptor in the SAID invasion pathway by assembling a multi-protein complex composed of parasite ligands RhopH3 and MSP1.
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