S100A8/A9 drives T cell exhaustion and compromises the therapeutic efficacy of bispecific antibodies in multiple myeloma.

Abstract Background: S100A8/A9 is a calcium-binding alarmin released during cellular stress and inflammation, modulating immune responses. We previously identified S100A8/A9 as a mediator of resistance to anti-BCMA CAR T-cell therapy through suppression of cytotoxic function. Here, we evaluate the role of S100A8/A9 in patients with multiple myeloma (MM) treated with bispecific antibodies (BsAb) targeting BCMA or GPRC5D. We perform in vitro and in-vivo validation to elucidate the underlying mechanisms contributing to suppression of T cell-directed therapy efficacy and test salvage strategies. Methods: Serum S100A8/A9 levels were correlated with depth of response (DOR) and progression-free survival (PFS) in patients receiving bispecific antibody therapy (n=19). We conducted extensive phenotyping of peripheral blood mononuclear cells (PBMCs) and quantified antigen-specific cytokine production and cytotoxicity by spectral flow cytometry. Post BsAb relapse EMD samples were interrogated with the Visium spatial transcriptomic platform. To study mechanistic effects, healthy donor T cells were incubated with recombinant S100A8/A9, and dynamic changes in phenotype, antigen-specific cytokine production, and cytotoxic activity were assessed. In vitro and in vivo salvage experiments were performed using blocking antibodies against S100A8/A9 in combination with bispecific therapeutics. Results: Patients with short PFS (n=11,<5 months, median 63 days) had significantly higher serum S100A8/A9 levels both at baseline and during therapy compared to those with longer PFS (n=8, median 503 days; p<0.05). S100A8/A9 levels during treatment inversely correlated with PFS (r=-0.52, p< 0.05). T cells from patients with short PFS exhibited features of exhaustion, including increased TOX+ CD3+ T cells (p=0.004) and higher CD8+ PD-1+ T cells. Upon stimulation with MM cell lines, PBMCs from these patients produced significantly lower levels of TNF-α, GM-CSF, IFN-γ, and IL-2 in both CD4+ and CD8+ subsets (p<0.05). CD4+ and CD8+ cytokine production inversely correlated with TOX expression (CD4+: r² = –0.6, p<0.05; CD8+: r² = –0.77, p<0.01). Antigen-specific cytotoxicity was significantly reduced in patients with short PFS compared to those with long PFS (p<0.001). Spatial transcriptomics from extramedullary collected samples showed colocalization of S100A8/A9 expressing CD14 monocytes with exhausted T cells in the tumor microenvironment of patients undergoing BsAb therapy. To measure the direct effect of S100A8/A9 on T cell functionality contributing to the impairment of T cell-directed therapy, we exposed healthy donor T cells to S100A8/A9. Incubation with S100A8/A9 induced T cell exhaustion in a dose-dependent manner, as evidenced by increased TOX+ CD4+ and TOX+ CD8+ populations, and impaired BsAb-mediated cytotoxicity. Importantly, blockade of anti- S100A8/A9 with monoclonal antibodies (mAbs) restored BsAb-mediated cytotoxicity (p=0.032) and prevented induction of TOX in healthy donor and patient samples, supporting a causal role of S100A8/A9 in T cell dysfunction. Direct incubation of T cells with S100A8/A9 caused a dose-dependent decrease in pERK signaling that was reversed with mAb salvage. In vivo treatment with anti-S100A8/A9 mAb activity showed a trend towards improved survival in combination with bispecific therapy as compared to bispecific therapy alone in transgenic tumor bearing mice. Conclusions: S100A8/A9 directly promotes T cell exhaustion and impairs T cell effector function, thereby reducing the efficacy of BsAb therapy in MM. Elevated serum S100A8/A9 levels are associated with inferior clinical responses and shorter PFS. Mechanistically, S100A8/A9 induces TOX expression and suppresses cytokine production and cytotoxicity in T cells. Salvage with monoclonal antibodies not only restores function but also prevents T cell exhaustion mediated by S100A8/A9 exposure. These findings position S100A8/A9 as a novel biomarker of resistance and a potential therapeutic target to enhance the efficacy of T cell-engaging immunotherapies in multiple myeloma.

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Journal
Blood
Published
2025-11-03
DOI
https://doi.org/10.1182/blood-2025-916
Primary Topic
S100 Proteins and Annexins
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article
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article

S100A8/A9 drives T cell exhaustion and compromises the therapeutic efficacy of bispecific antibodies in multiple myeloma.

Oliver Van Oekelen, José A. Martínez-Climent, Marta Larráyoz, Rahul Sanawar et al.
Blood
S100 Proteins and Annexins
article

S100A8/A9 drives T cell exhaustion and compromises the therapeutic efficacy of bispecific antibodies in multiple myeloma.

Oliver Van Oekelen, José A. Martínez-Climent, Marta Larráyoz, Rahul Sanawar, Cesar Rodriguez Valdes, Sundar Jagannath, Joshua Ryan Richter, Samir Sunil Parekh, Rudra Prasad Dutta, Junia Vieira, Amit Verma, Hearn Cho, Shambavi Richard, Adriana Rossi, Tarek H. Mouhieddine, Gurbakhash Kaur, Adolfo Aleman, Santiago Thibaud, Poulikos I. Poulikakos, Alessandro Laganà, Mani Mohindru, Mathieu Desaunay, Shriya Desai, Sidorela Reci, Leah Grossman, Rongbao Zhao, Larysa Sanchez
article en

Abstract

Abstract Background: S100A8/A9 is a calcium-binding alarmin released during cellular stress and inflammation, modulating immune responses. We previously identified S100A8/A9 as a mediator of resistance to anti-BCMA CAR T-cell therapy through suppression of cytotoxic function. Here, we evaluate the role of S100A8/A9 in patients with multiple myeloma (MM) treated with bispecific antibodies (BsAb) targeting BCMA or GPRC5D. We perform in vitro and in-vivo validation to elucidate the underlying mechanisms contributing to suppression of T cell-directed therapy efficacy and test salvage strategies. Methods: Serum S100A8/A9 levels were correlated with depth of response (DOR) and progression-free survival (PFS) in patients receiving bispecific antibody therapy (n=19). We conducted extensive phenotyping of peripheral blood mononuclear cells (PBMCs) and quantified antigen-specific cytokine production and cytotoxicity by spectral flow cytometry. Post BsAb relapse EMD samples were interrogated with the Visium spatial transcriptomic platform. To study mechanistic effects, healthy donor T cells were incubated with recombinant S100A8/A9, and dynamic changes in phenotype, antigen-specific cytokine production, and cytotoxic activity were assessed. In vitro and in vivo salvage experiments were performed using blocking antibodies against S100A8/A9 in combination with bispecific therapeutics. Results: Patients with short PFS (n=11,<5 months, median 63 days) had significantly higher serum S100A8/A9 levels both at baseline and during therapy compared to those with longer PFS (n=8, median 503 days; p<0.05). S100A8/A9 levels during treatment inversely correlated with PFS (r=-0.52, p< 0.05). T cells from patients with short PFS exhibited features of exhaustion, including increased TOX+ CD3+ T cells (p=0.004) and higher CD8+ PD-1+ T cells. Upon stimulation with MM cell lines, PBMCs from these patients produced significantly lower levels of TNF-α, GM-CSF, IFN-γ, and IL-2 in both CD4+ and CD8+ subsets (p<0.05). CD4+ and CD8+ cytokine production inversely correlated with TOX expression (CD4+: r² = –0.6, p<0.05; CD8+: r² = –0.77, p<0.01). Antigen-specific cytotoxicity was significantly reduced in patients with short PFS compared to those with long PFS (p<0.001). Spatial transcriptomics from extramedullary collected samples showed colocalization of S100A8/A9 expressing CD14 monocytes with exhausted T cells in the tumor microenvironment of patients undergoing BsAb therapy. To measure the direct effect of S100A8/A9 on T cell functionality contributing to the impairment of T cell-directed therapy, we exposed healthy donor T cells to S100A8/A9. Incubation with S100A8/A9 induced T cell exhaustion in a dose-dependent manner, as evidenced by increased TOX+ CD4+ and TOX+ CD8+ populations, and impaired BsAb-mediated cytotoxicity. Importantly, blockade of anti- S100A8/A9 with monoclonal antibodies (mAbs) restored BsAb-mediated cytotoxicity (p=0.032) and prevented induction of TOX in healthy donor and patient samples, supporting a causal role of S100A8/A9 in T cell dysfunction. Direct incubation of T cells with S100A8/A9 caused a dose-dependent decrease in pERK signaling that was reversed with mAb salvage. In vivo treatment with anti-S100A8/A9 mAb activity showed a trend towards improved survival in combination with bispecific therapy as compared to bispecific therapy alone in transgenic tumor bearing mice. Conclusions: S100A8/A9 directly promotes T cell exhaustion and impairs T cell effector function, thereby reducing the efficacy of BsAb therapy in MM. Elevated serum S100A8/A9 levels are associated with inferior clinical responses and shorter PFS. Mechanistically, S100A8/A9 induces TOX expression and suppresses cytokine production and cytotoxicity in T cells. Salvage with monoclonal antibodies not only restores function but also prevents T cell exhaustion mediated by S100A8/A9 exposure. These findings position S100A8/A9 as a novel biomarker of resistance and a potential therapeutic target to enhance the efficacy of T cell-engaging immunotherapies in multiple myeloma.

BloodVol. 146(Supplement 1)
Albert Einstein College of Medicine (US), Mount Sinai Hospital (US), ManRos Therapeutics (France) (FR), Ludwig Cancer Research (US), Universidad de Navarra (ES), Icahn School of Medicine at Mount Sinai (US)
Openalex Percentile: Top 65%
S100 Proteins and Annexins
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