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

Autor:	Luizet JB; Laboratory of Molecular Microbiology and Structural Biochemistry, CNRS UMR5086, Université de Lyon, 69367 Lyon, France., Raymond J; Laboratory of Molecular Microbiology and Structural Biochemistry, CNRS UMR5086, Université de Lyon, 69367 Lyon, France., Lacerda TLS; Laboratory of Molecular Microbiology and Structural Biochemistry, CNRS UMR5086, Université de Lyon, 69367 Lyon, France., Barbieux E; Department of Biology, Research Unit in Microorganisms Biology, Namur Research Institute for Life Sciences, 5000 Namur, Belgium.; Laboratory of Parasitology, Université Libre de Bruxelles Centre for Research in Immunology (UCRI), Université Libre de Bruxelles, 6041 Gosselies, Belgium., Kambarev S; Paul G. Allen School for Global Animal Health, Washington State University, Pullman, WA 99164., Bonici M; Laboratory of Molecular Microbiology and Structural Biochemistry, CNRS UMR5086, Université de Lyon, 69367 Lyon, France., Lembo F; Equipe labellisée Ligue 'Cell Polarity, Cell Signaling and Cancer', Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille Université, CNRS, INSERM, 13009 Marseille, France., Willemart K; Department of Biology, Research Unit in Microorganisms Biology, Namur Research Institute for Life Sciences, 5000 Namur, Belgium., Borg JP; Equipe labellisée Ligue 'Cell Polarity, Cell Signaling and Cancer', Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille Université, CNRS, INSERM, 13009 Marseille, France.; Institut Universitaire de France, 75231 Paris, France., Celli J; Paul G. Allen School for Global Animal Health, Washington State University, Pullman, WA 99164., Gérard FCA; Laboratory of Molecular Microbiology and Structural Biochemistry, CNRS UMR5086, Université de Lyon, 69367 Lyon, France., Muraille E; Department of Biology, Research Unit in Microorganisms Biology, Namur Research Institute for Life Sciences, 5000 Namur, Belgium.; Laboratory of Parasitology, Université Libre de Bruxelles Centre for Research in Immunology (UCRI), Université Libre de Bruxelles, 6041 Gosselies, Belgium., Gorvel JP; Centre d'Immunologie de Marseille-Luminy, CNRS, INSERM, Aix-Marseille Université, 13009 Marseille, France., Salcedo SP; Laboratory of Molecular Microbiology and Structural Biochemistry, CNRS UMR5086, Université de Lyon, 69367 Lyon, France; suzana.salcedo@ibcp.fr.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Aug 10; Vol. 118 (32).
DOI:	10.1073/pnas.2105324118
Abstrakt:	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. Competing Interests: The authors declare no competing interest.
Databáze:	MEDLINE
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