ArticleCell chemical biology2022
Ligand-induced interactions between butyrophilin 2A1 and 3A1 internal domains in the HMBPP receptor complex.
Article in Cell chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 48 citations in OpenAlex.
- Insights into the Mechanism of Action of Phosphoantigen Prodrugs on Vγ9Vδ2 T Cell Activation.ACS pharmacology & translational science · 2026Article
- Review
- NanoBRET Saturation Analysis with a Novel HaloTag Ligand Reveals Butyrophilin Heteromeric Interactions Controlling γ9δ2 T Cell Activation.ACS chemical biology · 2026Article
- Benzoic Acid Derivatives Improve Plasma Stability of Diester Butyrophilin Ligand Prodrugs.Journal of medicinal chemistry · 2026Article
- Cell stress activates γ9δ2 T cells via endogenous phosphoantigens and butyrophilin complex dynamics.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2026Article
- Vγ9Vδ2 T cells in tuberculosis: protective immunity and translational perspectives.Frontiers in immunology · 2026Review
- γ9δ2 T cells detect mevalonate diphosphate via BTN3A3.Cellular and molecular life sciences : CMLS · 2025Article
- Disrupting the balance between activating and inhibitory receptors of γδT cells for effective cancer immunotherapy.Nature reviews. Cancer · 2025Review
- A Brief Molecular History of Vγ9Vδ2 TCR-Mediated Phosphoantigen Sensing.Immunological reviews · 2025Review
- Mapping the extracellular molecular architecture of the pAg-signaling complex with α-Butyrophilin antibodies.Scientific reports · 2025Article
- Synthesis and evaluation of triazole-containing aryl/acyloxy prodrugs of a BTN3A1 ligand.European journal of medicinal chemistry · 2025Article
- Investigation of structural and dynamic properties of the Butyrophilin BTN3A1/BTN2A1 cytoplasmic complex byFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Gamma delta T cells and their immunotherapeutic potential in cancer.Biomarker research · 2025Review
- Central memory-enriched Vγ9Vδ2 γδ T cells via TGF-β expansion demonstrate enhancedFrontiers in immunology · 2025Article
- Enhanced Plasma Stability and Potency of Aryl/Acyloxy Prodrugs of a BTN3A1 Ligand.ACS medicinal chemistry letters · 2024Article
- Synthesis and evaluation of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate analogs as competitive partial agonists of butyrophilin 3A1.European journal of medicinal chemistry · 2024Article
- Cancer immunotherapy by γδ T cells.Science (New York, N.Y.) · 2024Review
- Low frequency of Vγ9Vδ2 T cells predicts poor survival in newly diagnosed acute myeloid leukemia.Blood advances · 2024Article
- Vγ9Vδ2 T cells recognize butyrophilin 2A1 and 3A1 heteromers.Nature immunology · 2024Article
- Phosphonodiamidate prodrugs of phosphoantigens (ProPAgens) exhibit potent Vγ9/Vδ2 T cell activation and eradication of cancer cells.RSC medicinal chemistry · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The ligand-bound (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate (HMBPP) receptor (BTN3A1 and BTN2A1) is detectable by the T cell receptor (TCR) of Vγ9Vδ2 T cells. Although BTN3A1 binds to phosphoantigens (pAgs), the mechanisms resulting in receptor activation are not clear. We used CRISPR-Cas9, ELISA, nano-bioluminescence resonance energy transfer (BRET), and isothermal titration calorimetry (ITC) to evaluate the role of BTN2A1. Depletion of BTN2A1 and rescue experiments demonstrate that its internal domain is essential for pAg detection. Internal hetero-BRET signals are observed between BTN2A1 and BTN3A1 that are increased by pAg. ITC detects a direct interaction between the intracellular domains of BTN3A1 and BTN2A1 only in the presence of pAg. This interaction is abrogated by removal of the BTN2A1 juxtamembrane (JM) region but not by removal of the BTN3A1 JM region. Regional mutations between BTN2A1 316-326 clearly affect the interferon γ (IFNγ) response and hetero-BRET signal. Mutations to amino acids L318, W320, and L325 indicate that these amino acids are crucial. This study demonstrates a pAg-inducible interaction between BTN2A1 and BTN3A1 internal domains.
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