ArticleNature communications2024
Structural basis for IL-33 recognition and its antagonism by the helminth effector protein HpARI2.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Parasites and allergies: a complex bidirectional relationship from evolutionary origins to modern therapeutics.Antonie van Leeuwenhoek · 2026Review
- IL-33/ST2 Signaling Sustains Hepato-Intestinal Homeostasis by Orchestrating Vascular Surveillance and Immune Regulatory Circuits During Experimental Trypanosoma cruzi Infection.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Gastrointestinal tuft cells: Recent insights and next questions.Science immunology · 2026Review
- Interleukin-33-Mediated Mechanical-Loading Induced Degeneration of Knee Joint Chondrocytes.FASEB bioAdvances · 2025Article
- Modulation of the Immune Response by Nematode Derived Molecules.International journal of molecular sciences · 2025Review
- Vaccination against helminth IL-33 modulators permits immune-mediated parasite ejection.Cell reports · 2025Article
- Cytokines from parasites: manipulating host responses by molecular mimicry.The Biochemical journal · 2025Review
- Article
- IL-33-binding HpARI family homologues with divergent effects in suppressing or enhancing type 2 immune responses.Infection and immunity · 2024Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
IL-33 plays a significant role in inflammation, allergy, and host defence against parasitic helminths. The model gastrointestinal nematode Heligmosomoides polygyrus bakeri secretes the Alarmin Release Inhibitor HpARI2, an effector protein that suppresses protective immune responses and asthma in its host by inhibiting IL-33 signalling. Here we reveal the structure of HpARI2 bound to mouse IL-33. HpARI2 contains three CCP-like domains, and we show that it contacts IL-33 primarily through the second and third of these. A large loop which emerges from CCP3 directly contacts IL-33 and structural comparison shows that this overlaps with the binding site on IL-33 for its receptor, ST2, preventing formation of a signalling complex. Truncations of HpARI2 which lack the large loop from CCP3 are not able to block IL-33-mediated signalling in a cell-based assay and in an in vivo female mouse model of asthma. This shows that direct competition between HpARI2 and ST2 is responsible for suppression of IL-33-dependent responses.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.