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nature portfolio vh/vλ cdna libraries privacy policy t-cell-mediated anti-tumor immunity1 org/mus_musculus/info/index org/homo_sapiens/info/index short-insert cdna library advertising direct perforin/granzyme-dependent killing pgc-1alpha-responsive genes involved h2-ld/ah1 tetramer coupled anti-cd3/cd28 coated beads thermofischer scientific org/gsea/msigdb/cards/hallmark_interferon_gamma_response org/gsea/msigdb/cards/hallmark_inflammatory_response org/gsea/msigdb/cards/hallmark_il2_stat5_signaling org/gsea/msigdb/cards/hallmark_tgf_beta_signaling org/gsea/msigdb/cards/hallmark_tnfa_signaling_via_nfkb org/gsea/msigdb/cards/hallmark_spermatogenesis social media integrin αvβ8 interacts european research council nature 474 nature 554 nature reprints anti-pd-l1 antibody avelumab platelet-specific-garp ko mice research-aimed surgery inhibit tgf-β1-dependent immunosuppression received research support tgf-β1 fcd + anti-pd-1 combination treg-derived tgf-β1 activity anti-tgf-β neutralizes activity garp/tgf-beta1 complexes inhibit induces immune-mediated rejections formalin-fixed paraffin-embedded cell-mediated immunosuppression orchestrated psmad2/β-actin signals relative regulatory cell-mediated suppression impaired t-cell functionality anti-cd3/28 coated beads pd-1-expressing anti-tumor cd8+ mc38-bearing garpysg/ysg mice ah1/h-2ld tetramer ethique biomédicale hospitalo-facultaire author information authors pd-1/pd-l1 blockade blocks tgf-β1 activation latent tgf-beta structure

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      headline:Selective inhibition of TGF-β1 produced by GARP-expressing Tregs overcomes resistance to PD-1/PD-L1 blockade in cancer
      description:TGF-β1, β2 and β3 bind a common receptor to exert vastly diverse effects in cancer, supporting either tumor progression by favoring metastases and inhibiting anti-tumor immunity, or tumor suppression by inhibiting malignant cell proliferation. Global TGF-β inhibition thus bears the risk of undesired tumor-promoting effects. We show that selective blockade of TGF-β1 production by Tregs with antibodies against GARP:TGF-β1 complexes induces regressions of mouse tumors otherwise resistant to anti-PD-1 immunotherapy. Effects of combined GARP:TGF-β1/PD-1 blockade are immune-mediated, do not require FcγR-dependent functions and increase effector functions of anti-tumor CD8+ T cells without augmenting immune cell infiltration or depleting Tregs within tumors. We find GARP-expressing Tregs and evidence that they produce TGF-β1 in one third of human melanoma metastases. Our results suggest that anti-GARP:TGF-β1 mAbs, by selectively blocking a single TGF-β isoform emanating from a restricted cellular source exerting tumor-promoting activity, may overcome resistance to PD-1/PD-L1 blockade in patients with cancer. Inhibiting TGF-β1 to increase immune responses against tumors bears the risk of tumor-promoting toxicity. Here the authors show that selectively blocking TGF-β1 produced by immunosuppressive cells is feasible with anti-GARP:TGF-β1 antibodies and improves the efficacy of PD-1 blockade immunotherapy.
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      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
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      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium
      name:de Duve Institute, Université catholique de Louvain, Brussels, Belgium

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