Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer

G protein-coupled receptors (GPCRs) are significant drug targets, but their potential in cancer therapy remains underexplored. Conventional GPCR agonists or antagonists have shown limited effectiveness in cancer treatment, necessitating new GPCR-targeting strategies for more effective therapies. Thi...

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Main Authors: Yunjun Ge, Huiwen Guan, Ting Li, Jie Wang, Liang Ying, Shuhui Guo, Jinjian Lu, Richard D. Ye, Guosheng Wu
Format: Article
Language:English
Published: Elsevier 2025-07-01
Series:Acta Pharmaceutica Sinica B
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Online Access:http://www.sciencedirect.com/science/article/pii/S2211383525002977
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author Yunjun Ge
Huiwen Guan
Ting Li
Jie Wang
Liang Ying
Shuhui Guo
Jinjian Lu
Richard D. Ye
Guosheng Wu
author_facet Yunjun Ge
Huiwen Guan
Ting Li
Jie Wang
Liang Ying
Shuhui Guo
Jinjian Lu
Richard D. Ye
Guosheng Wu
author_sort Yunjun Ge
collection DOAJ
description G protein-coupled receptors (GPCRs) are significant drug targets, but their potential in cancer therapy remains underexplored. Conventional GPCR agonists or antagonists have shown limited effectiveness in cancer treatment, necessitating new GPCR-targeting strategies for more effective therapies. This study discovers that Yersinia pestis LcrV, a crucial linker protein for plague infection, acts as a biased agonist of a GPCR, the formyl peptide receptor 1 (FPR1). The LcrV protein induces unique conformational changes in FPR1, resulting in G proteins being activated in a distinctive state without subunit dissociation. This leads to a biased signaling profile characterized by cyclic adenosine monophosphate (cAMP) responses and β-arrestin2 recruitment, but not calcium mobilization. In FPR1-expressing triple-negative breast cancer (TNBC) cells, LcrV bi-directionally modulates intracellular signaling pathways, downregulating extracellular signal-regulated kinases (ERK1/2) and Akt pathways while upregulating Jun N-terminal kinase (JNK) and p38 pathways. This dual modulation results in cell cycle arrest and the inhibition of TNBC cell proliferation. In TNBC xenograft mouse models, long-term LcrV treatment inhibits tumor growth more effectively than a conventional FPR1 antagonist. Additionally, LcrV treatment reprograms tumor cells by reducing stemness-associated proteins OCT4 and c-MYC. Our findings highlight the potential of biased GPCR agonists as a novel GPCR-targeting strategy for cancer treatment.
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spelling doaj-art-9f66efca31da412d9a29dac085e9f1442025-08-20T03:50:06ZengElsevierActa Pharmaceutica Sinica B2211-38352025-07-011573646366210.1016/j.apsb.2025.04.030Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancerYunjun Ge0Huiwen Guan1Ting Li2Jie Wang3Liang Ying4Shuhui Guo5Jinjian Lu6Richard D. Ye7Guosheng Wu8Department of Basic Medical Science, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu 214122, China; MoE Medical Basic Research Innovation Center for Gut Microbiota and Chronic Diseases, School of Medicine, Wuxi 214122, China; Corresponding authors.Department of Basic Medical Science, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu 214122, China; MoE Medical Basic Research Innovation Center for Gut Microbiota and Chronic Diseases, School of Medicine, Wuxi 214122, ChinaState Key Laboratory for Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macau SAR 999078, China; MoE Frontiers Science Center for Precision Oncology, University of Macau, Macau SAR 999078, ChinaDepartment of Basic Medical Science, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu 214122, China; MoE Medical Basic Research Innovation Center for Gut Microbiota and Chronic Diseases, School of Medicine, Wuxi 214122, ChinaDepartment of Basic Medical Science, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu 214122, China; MoE Medical Basic Research Innovation Center for Gut Microbiota and Chronic Diseases, School of Medicine, Wuxi 214122, ChinaShenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518172, ChinaState Key Laboratory for Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macau SAR 999078, China; MoE Frontiers Science Center for Precision Oncology, University of Macau, Macau SAR 999078, ChinaKobilka Institute of Innovative Drug Discovery, School of Medicine, the Chinese University of Hong Kong, Shenzhen 518172, China; Corresponding authors.Department of Basic Medical Science, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu 214122, China; MoE Medical Basic Research Innovation Center for Gut Microbiota and Chronic Diseases, School of Medicine, Wuxi 214122, China; Corresponding authors.G protein-coupled receptors (GPCRs) are significant drug targets, but their potential in cancer therapy remains underexplored. Conventional GPCR agonists or antagonists have shown limited effectiveness in cancer treatment, necessitating new GPCR-targeting strategies for more effective therapies. This study discovers that Yersinia pestis LcrV, a crucial linker protein for plague infection, acts as a biased agonist of a GPCR, the formyl peptide receptor 1 (FPR1). The LcrV protein induces unique conformational changes in FPR1, resulting in G proteins being activated in a distinctive state without subunit dissociation. This leads to a biased signaling profile characterized by cyclic adenosine monophosphate (cAMP) responses and β-arrestin2 recruitment, but not calcium mobilization. In FPR1-expressing triple-negative breast cancer (TNBC) cells, LcrV bi-directionally modulates intracellular signaling pathways, downregulating extracellular signal-regulated kinases (ERK1/2) and Akt pathways while upregulating Jun N-terminal kinase (JNK) and p38 pathways. This dual modulation results in cell cycle arrest and the inhibition of TNBC cell proliferation. In TNBC xenograft mouse models, long-term LcrV treatment inhibits tumor growth more effectively than a conventional FPR1 antagonist. Additionally, LcrV treatment reprograms tumor cells by reducing stemness-associated proteins OCT4 and c-MYC. Our findings highlight the potential of biased GPCR agonists as a novel GPCR-targeting strategy for cancer treatment.http://www.sciencedirect.com/science/article/pii/S2211383525002977G protein-coupled receptorYersinia LcrVBiased agonistFormyl peptide receptor 1G proteinConformational change
spellingShingle Yunjun Ge
Huiwen Guan
Ting Li
Jie Wang
Liang Ying
Shuhui Guo
Jinjian Lu
Richard D. Ye
Guosheng Wu
Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer
Acta Pharmaceutica Sinica B
G protein-coupled receptor
Yersinia LcrV
Biased agonist
Formyl peptide receptor 1
G protein
Conformational change
title Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer
title_full Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer
title_fullStr Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer
title_full_unstemmed Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer
title_short Discovery of Yersinia LcrV as a novel biased agonist of formyl peptide receptor 1 to bi-directionally modulate intracellular kinases in triple-negative breast cancer
title_sort discovery of yersinia lcrv as a novel biased agonist of formyl peptide receptor 1 to bi directionally modulate intracellular kinases in triple negative breast cancer
topic G protein-coupled receptor
Yersinia LcrV
Biased agonist
Formyl peptide receptor 1
G protein
Conformational change
url http://www.sciencedirect.com/science/article/pii/S2211383525002977
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