ArticleNature communications2023
Plasmodium falciparum has evolved multiple mechanisms to hijack human immunoglobulin M.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Reconstruction of the Flexible IgM Fc Core Using Atomic Force Microscopy Topography and the AFM-Assembly Pipeline.Journal of molecular recognition : JMR · 2026Article
- The resistance to Toxoplasma gondii in Microtus fortis is associated with the activation of the complement lectin pathway.PLoS neglected tropical diseases · 2026Article
- Human FcRL5 is an Fc receptor that simultaneously engages two IgGs.Science advances · 2026Article
- Naturally acquired antibodies toFrontiers in immunology · 2026Article
- Dietary supplementation withFrontiers in microbiology · 2026Article
- Article
- Changes in growth performance, immune function, and meat quality of yellow-feathered broilers fedFrontiers in veterinary science · 2025Article
- Identification of novel PfEMP1 variants containing domain cassettes 11, 15 and 8 that mediate the Plasmodium falciparum virulence-associated rosetting phenotype.PLoS pathogens · 2025Article
- Effects of Dietary Schizochytrium Algae as ω-3 PUFA Source on the Egg-Laying Quail Performance, Serum Indexes, and Egg Yolk Fatty Acids Contents.Animals : an open access journal from MDPI · 2024Article
- CD5L associates with IgM via the J chain.Nature communications · 2024Article
- PfEMP1 and var genes - Still of key importance in Plasmodium falciparum malaria pathogenesis and immunity.Advances in parasitology · 2024Review
- Variable Surface Antigens ofProtein and peptide letters · 2024Review
- Cryo-electron microscopy of IgM-VAR2CSA complex reveals IgM inhibits binding of Plasmodium falciparum to Chondroitin Sulfate A.Nature communications · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasmodium falciparum causes the most severe malaria in humans. Immunoglobulin M (IgM) serves as the first line of humoral defense against infection and potently activates the complement pathway to facilitate P. falciparum clearance. A number of P. falciparum proteins bind IgM, leading to immune evasion and severe disease. However, the underlying molecular mechanisms remain unknown. Here, using high-resolution cryo-electron microscopy, we delineate how P. falciparum proteins VAR2CSA, TM284VAR1, DBLMSP, and DBLMSP2 target IgM. Each protein binds IgM in a different manner, and together they present a variety of Duffy-binding-like domain-IgM interaction modes. We further show that these proteins interfere directly with IgM-mediated complement activation in vitro, with VAR2CSA exhibiting the most potent inhibitory effect. These results underscore the importance of IgM for human adaptation of P. falciparum and provide critical insights into its immune evasion mechanism.
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