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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 6

PC downregulates PD-L1 expression via targeting SYVN1.

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PC downregulates PD-L1 expression via targeting SYVN1.
(A–C) Following S...
(A–C) Following SYVN1 knockdown in RKO cells, Western blotting detected PD-L1 protein levels after PC treatment (A). si, siRNA. SYVN1 knockdown efficiency was validated by RT-qPCR (B). (C) Quantification of A. (D) Western blotting analysis of PD-L1 protein expression in RKO cells overexpressing SYVN1 and cocultured with PC. (E) Quantification of D. (F–H) RKO cells with SYVN1 knockdown (F), SYVN1 overexpression (G), or PD-L1 knockdown (H) were cocultured with PD-1–overexpressing Jurkat cells (activated with PHA/PMA) at a 9:1 E:T ratio for 24 hours, in the presence or absence of PC, to assess tumor cell killing. The remaining RKO cells were stained with crystal violet and imaged (Cytation 5; scale bar: 100 μm). (I) SYVN1 knockdown efficiency was measured by RT-qPCR. (J) Quantification of F. (K) SYVN1 overexpression was verified by Western blotting and quantified. (L) Quantification of G. (M) PD-L1 knockdown efficiency was measured by RT-qPCR. (N) Quantification of H. (O–Q) PC binding to SYVN1 was demonstrated by CETSA at graded temperatures (O) and a fixed 45°C with different PC doses (P) and by the drug affinity responsive target stability assay under various PC concentrations (1:300 ratio) (Q). (R and S) Molecular docking of PC with SYVN1. (T–W) MST assay of GFP-tagged SYVN1 cells overexpressing WT SYVN1 (M) or SYVN1 mutants (Trp118A, Glu121A, and Glu87A) (N–P). (X and Y) Immunoprecipitation experiments confirmed that PC enhances the interaction between the PD-L1 and SYVN1 proteins. Cell lysates were co-precipitated using antibodies against PD-L1 (X) or SYVN1 (Y). The data shown are the mean ± SEM of triplicate experiments. (B, I, K, M) Significance was determined using Student’s t test; (O) 2-way ANOVA with Šídák multiple comparisons test; All other panels: 1-way ANOVA with Dunnett multiple comparisons 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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