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Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2021

The Brucella effector BspL targets the ER-associated degradation (ERAD) pathway and delays bacterial egress from infected cells

Jean Celli

Résumé

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.

Dates et versions

hal-03565955 , version 1 (11-02-2022)

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Citer

Jean-Baptiste Luizet, Julie Raymond, Thais Lourdes Santos Lacerda, Emeline Barbieux, Stanimir Kambarev, et al.. The Brucella effector BspL targets the ER-associated degradation (ERAD) pathway and delays bacterial egress from infected cells. Proceedings of the National Academy of Sciences of the United States of America, 2021, 118 (32), pp.e2105324118. ⟨10.1073/pnas.2105324118⟩. ⟨hal-03565955⟩
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