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Harly, Christelle; Guillaume, Yves; Nedellec, Steven; Peigné, Cassie-Marie; Mönkkönen, Hannu; Mönkkönen, Jukka; Li, Jianqiang; Kuball, Jürgen; Adams, Erin J.; Netzer, Sonia; Déchanet-Merville, Julie; Léger, Alexandra; Herrmann, Thomas; Breathnach, Richard; Olive, Daniel; Bonneville, Marc; Scotet, Emmanuel
Blood, 09/2012, Letnik: 120, Številka: 11Journal Article
Human peripheral Vγ9Vδ2 T cells are activated by phosphorylated metabolites (phosphoagonists PAg) of the mammalian mevalonate or the microbial desoxyxylulose-phosphate pathways accumulated by infected or metabolically distressed cells. The underlying mechanisms are unknown. We show that treatment of nonsusceptible target cells with antibody 20.1 against CD277, a member of the extended B7 superfamily related to butyrophilin, mimics PAg-induced Vγ9Vδ2 T-cell activation and that the Vγ9Vδ2 T-cell receptor is implicated in this effect. Vγ9Vδ2 T-cell activation can be abrogated by exposing susceptible cells (tumor and mycobacteria-infected cells, or aminobisphosphonate-treated cells with up-regulated PAg levels) to antibody 103.2 against CD277. CD277 knockdown and domain-shuffling approaches confirm the key implication of the CD277 isoform BTN3A1 in PAg sensing by Vγ9Vδ2 T cells. Fluorescence recovery after photobleaching (FRAP) experiments support a causal link between intracellular PAg accumulation, decreased BTN3A1 membrane mobility, and ensuing Vγ9Vδ2 T-cell activation. This study demonstrates a novel role played by B7-like molecules in human γδ T-cell antigenic activation and paves the way for new strategies to improve the efficiency of immunotherapies using Vγ9Vδ2 T cells.
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