ArticleThe Journal of biological chemistry2016
Binding of Plasmodium falciparum Merozoite Surface Proteins DBLMSP and DBLMSP2 to Human Immunoglobulin M Is Conserved among Broadly Diverged Sequence Variants.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Module-level recombination drives DBLMSP polymorphism and functional conservation in Plasmodium falciparum.Parasite (Paris, France) · 2026Article
- Article
- Role for gene conversion in the evolution of cell-surface antigens of the malaria parasite Plasmodium falciparum.PLoS biology · 2024Article
- Plasmodium falciparum has evolved multiple mechanisms to hijack human immunoglobulin M.Nature communications · 2023Article
- Plasmodium falciparum merozoite invasion ligands, linked antimalarial resistance loci and ex vivo responses to antimalarials in The Gambia.The Journal of antimicrobial chemotherapy · 2022Article
- Article
- Naturally acquired antibody kinetics against Plasmodium vivax antigens in people from a low malaria transmission region in western Thailand.BMC medicine · 2022Article
- Gramtools enables multiscale variation analysis with genome graphs.Genome biology · 2021Article
- An open dataset ofWellcome open research · 2021Article
- Plasma mEV levels in Ghanain malaria patients with low parasitaemia are higher than those of healthy controls, raising the potential for parasite markers in mEVs as diagnostic targets.Journal of extracellular vesicles · 2020Article
- IgM in human immunity toScience advances · 2019Article
- Reverse immunodynamics: a new method for identifying targets of protective immunity.Scientific reports · 2019Article
- A library of recombinant Babesia microti cell surface and secreted proteins for diagnostics discovery and reverse vaccinology.International journal for parasitology · 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
- An expanded global inventory of allelic variation in the most extremely polymorphic region of Plasmodium falciparum merozoite surface protein 1 provided by short read sequence data.Malaria journal · 2018Article
- Molecular Camouflage of Plasmodium falciparum Merozoites by Binding of Host Vitronectin to P47 Fragment of SERA5.Scientific reports · 2018Article
- Proteome-wide mapping of immune features onto Plasmodium protein three-dimensional structures.Scientific reports · 2018Article
- Malaria Parasites: The Great Escape.Frontiers in immunology · 2016Review
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Authors and funding
16 authors at 5 institutions in 1 country.
Funding
Abstract
Diversity at pathogen genetic loci can be driven by host adaptive immune selection pressure and may reveal proteins important for parasite biology. Population-based genome sequencing of Plasmodium falciparum, the parasite responsible for the most severe form of malaria, has highlighted two related polymorphic genes called dblmsp and dblmsp2, which encode Duffy binding-like (DBL) domain-containing proteins located on the merozoite surface but whose function remains unknown. Using recombinant proteins and transgenic parasites, we show that DBLMSP and DBLMSP2 directly and avidly bind human IgM via their DBL domains. We used whole genome sequence data from over 400 African and Asian P. falciparum isolates to show that dblmsp and dblmsp2 exhibit extreme protein polymorphism in their DBL domain, with multiple variants of two major allelic classes present in every population tested. Despite this variability, the IgM binding function was retained across diverse sequence representatives. Although this interaction did not seem to have an effect on the ability of the parasite to invade red blood cells, binding of DBLMSP and DBLMSP2 to IgM inhibited the overall immunoreactivity of these proteins to IgG from patients who had been exposed to the parasite. This suggests that IgM binding might mask these proteins from the host humoral immune system.
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