内质网相关蛋白降解
细胞生物学
内质网
效应器
生物
未折叠蛋白反应
液泡
细胞内
细胞内寄生虫
布鲁氏菌
免疫学
细胞质
布鲁氏菌病
作者
Jean-Baptiste Luizet,Julie Raymond,Thaís Lourdes Santos Lacerda,Emeline Barbieux,Stanimir Kambarev,Magali Bonici,Frédérique Lembo,Kévin Willemart,Jean-Paul Borg,Jean Celli,Francine C A Gérard,Eric Muraille,Jean‐Pierre Gorvel,Suzana P. Salcedo
标识
DOI:10.1073/pnas.2105324118
摘要
Perturbation of the endoplasmic reticulum (ER), a central organelle of the cell, can have critical consequences for cellular homeostasis. An elaborate surveillance system known as ER quality control ensures that cells can respond and adapt to stress via the unfolded protein response (UPR) and that only correctly assembled proteins reach their destination. Interestingly, several bacterial pathogens hijack the ER to establish an infection. However, it remains poorly understood how bacterial pathogens exploit ER quality-control functions to complete their intracellular cycle. Brucella spp. replicate extensively within an ER-derived niche, which evolves into specialized vacuoles suited for exit from infected cells. Here we present Brucella-secreted protein L (BspL), a Brucella abortus effector that interacts with Herp, a central component of the ER-associated degradation (ERAD) machinery. We found that BspL enhances ERAD at the late stages of the infection. BspL targeting of Herp and ERAD allows tight control of the kinetics of autophagic Brucella-containing vacuole formation, delaying the last step of its intracellular cycle and cell-to-cell spread. This study highlights a mechanism by which a bacterial pathogen hijacks ERAD components for fine regulation of its intracellular trafficking.
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