ArticleACS chemical biology2026
NanoBRET Saturation Analysis with a Novel HaloTag Ligand Reveals Butyrophilin Heteromeric Interactions Controlling γ9δ2 T Cell Activation.
Article in ACS chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Human γ9δ2 T cells detect microbial phosphoantigens (pAg) through butyrophilin (BTN) family proteins; however, how multiple BTN paralogs assemble into functional signaling complexes remains unresolved. Because γ9δ2 T cell activation requires coordinated action of several BTN members rather than a single receptor pair, defining their organization in living cells is essential. Here, we apply a live-cell NanoBRET saturation analysis using a novel HaloTag ligand to quantitatively resolve BTN oligomerization dynamics. We found that BTN3A1 exists as higher-order basal oligomers. Coexpression of BTN3A2 or BTN3A3 redistributes these assemblies into defined BTN3 dimers. The BTN3 dimers have a baseline interaction with BTN2A1 dimers that is altered by IgV domain interactions and by classical pAgs such as (
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