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Proanthocyanidins enhance antitumor immunity by promoting ubiquitin-proteasomal PD-L1 degradation via stabilization of LKB1 and SYVN1
Mengting Xu, Xuwen Lin, Hanchi Xu, Hongmei Hu, Xinying Xue, Qing Zhang, Dianping Yu, Saisai Tian, Mei Xie, Linyang Li, Xiaoyu Tao, Xinru Li, Simeng Li, Shize Xie, Yating Tian, Xia Liu, Hanchen Xu, Qun Wang, Weidong Zhang, Sanhong Liu
Mengting Xu, Xuwen Lin, Hanchi Xu, Hongmei Hu, Xinying Xue, Qing Zhang, Dianping Yu, Saisai Tian, Mei Xie, Linyang Li, Xiaoyu Tao, Xinru Li, Simeng Li, Shize Xie, Yating Tian, Xia Liu, Hanchen Xu, Qun Wang, Weidong Zhang, Sanhong Liu
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Research Article Immunology Oncology

Proanthocyanidins enhance antitumor immunity by promoting ubiquitin-proteasomal PD-L1 degradation via stabilization of LKB1 and SYVN1

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Abstract

Programmed cell death 1 ligand 1–targeted (PD-L1–targeted) immune checkpoint inhibitors are revolutionizing cancer therapy. However, strategies to induce endogenous PD-L1 degradation represent an emerging therapeutic paradigm. Here, we identified proanthocyanidins (PC) as a potent inducer of PD-L1 degradation through an endoplasmic reticulum–associated degradation (ERAD) mechanism. Mechanistically, PC exerted dual effects: First, it targeted and stabilized LKB1 to activate AMPK in tumor cells, subsequently inducing the phosphorylation of PD-L1 at Ser195 — a disruption that in turn impaired glycosylation of PD-L1 and promoted its retention in the ER. Second, PC directly bound to the E3 ubiquitin ligase SYVN1 to increase its protein stability, which strengthened PD-L1–SYVN1 binding, thereby accelerating K48-linked ubiquitination and proteasomal degradation of ER-retained PD-L1. This cascade culminated in the activation of CD8+ T cell–dominated antitumor immune responses, accompanied by suppression of myeloid-derived suppressor cells and regulatory T cells. In preclinical models of lung and colorectal cancer, PC exhibited synergistic antitumor efficacy when combined with anti–cytotoxic T lymphocyte antigen 4 (anti–CTLA-4) antibodies. Notably, PC also potently inhibited the progression of azoxymethane/dextran sodium sulfate–induced orthotopic colorectal cancer in mice. Collectively, our findings unveil an antitumor mechanism of PC, establishing this small-molecule compound as an ERAD pathway–exploiting immune checkpoint modulator with promising translational potential for cancer therapy.

Authors

Mengting Xu, Xuwen Lin, Hanchi Xu, Hongmei Hu, Xinying Xue, Qing Zhang, Dianping Yu, Saisai Tian, Mei Xie, Linyang Li, Xiaoyu Tao, Xinru Li, Simeng Li, Shize Xie, Yating Tian, Xia Liu, Hanchen Xu, Qun Wang, Weidong Zhang, Sanhong Liu

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Figure 5

PC promotes K48-linked polyubiquitination of PD-L1 for its degradation.

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PC promotes K48-linked polyubiquitination of PD-L1 for its degradation.
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(A–D) RKO (A) and H1975 (C) cells were cotreated with 60 μg/mL CHX and 40 μM PC. The PD-L1 protein expression was detected by Western blot at 0, 1, 3, 6, and 9 hours posttreatment. Quantification is shown in B and D. (E–L) RKO cells were treated with different concentrations of the following compounds and 40 μM PC: eeyarestatin I (EI; 10, 20 μM), MG132 (1, 5 μM), chloroquine (CQ; 20, 40 μM), or 3-methyladenine (3-MA; 1, 5 mM). The expression of PD-L1 was subsequently examined via Western blotting (E–H) and flow cytometry (I–L), followed by statistical analysis. (M and N) PD-L1 expression was detected by immunofluorescence in RKO cells cotreated with 40 μM PC and either 5 μM MG-132 or 40 μM CQ. Blue fluorescence indicates cell nuclei, whereas red fluorescence indicates PD-L1 levels on the cell membrane. Scale bars of 100 μm, 200 μm, and 400 μm were used. (N) Quantitative analysis. (O) PD-L1 was immunoprecipitated from PC-treated RKO cell lysates, and the level of ubiquitination was assessed via Western blotting with a ubiquitin (Ub) antibody. (P and Q) C57BL/6 mice subcutaneously transplanted with MC38 (P) or Lewis (Q) cells were treated with different doses of PC. Western blotting with an anti-Ub antibody was used to detect PD-L1 ubiquitination in tumor tissues. (R) RKO cells expressing WT ubiquitin (WT-Ub), K48R-Ub, or K63R-Ub were treated with PC. After immunoprecipitation with an anti–PD-L1 antibody, PD-L1 ubiquitination was analyzed via Western blotting with an anti-Ub antibody. The data shown are the mean ± SEM of triplicate experiments. Statistical differences were determined by 1-way ANOVA with Dunnett’s multiple-comparison test. *P < 0.05, **P < 0.01, and ****P < 0.0001.

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ISSN: 0021-9738 (print), 1558-8238 (online)

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