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Bioid screen of salmonella type 3 secreted ...
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Document type :
Article dans une revue scientifique: Article original
DOI :
10.1038/s41564-019-0580-9
PMID :
31611645
Permalink :
http://hdl.handle.net/20.500.12210/74998
Title :
Bioid screen of salmonella type 3 secreted effectors reveals host factors involved in vacuole positioning and stability during infection
Author(s) :
D'costa, Vanessa M. [Auteur]
Coyaud, Etienne-Marie [Auteur]
Boddy, Kirsten C. [Auteur]
Laurent, Estelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
St-Germain, Jonathan R. [Auteur]
Li, Taoyingnan [Auteur]
Grinstein, Sergio [Auteur]
Raught, Brian [Auteur]
Brumell, John H. [Auteur]
Journal title :
Nature microbiology
Abbreviated title :
NAT. MICROBIOL
Volume number :
4
Pages :
-
Publication date :
2019-12-01
ISSN :
2058-5276
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
Many bacterial pathogens express virulence proteins that are translocated into host cells (herein referred to as effectors), where they can interact with target proteins to manipulate host cell processes. These effector-host ...
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Many bacterial pathogens express virulence proteins that are translocated into host cells (herein referred to as effectors), where they can interact with target proteins to manipulate host cell processes. These effector-host protein interactions are often dynamic and transient in nature, making them difficult to identify using traditional interaction-based methods. Here, we performed a systematic comparison between proximity-dependent biotin labelling (BioID) and immunoprecipitation coupled with mass spectrometry to investigate a series of Salmonella type 3 secreted effectors that manipulate host intracellular trafficking (SifA, PipB2, SseF, SseG and SopD2). Using BioID, we identified 632 candidate interactions with 381 unique human proteins, collectively enriched for roles in vesicular trafficking, cytoskeleton components and transport activities. From the subset of proteins exclusively identified by BioID, we report that SifA interacts with BLOC-2, a protein complex that regulates dynein motor activity. We demonstrate that the BLOC-2 complex is necessary for SifA-mediated positioning of Salmonella-containing vacuoles, and affects stability of the vacuoles during infection. Our study provides insight into the coordinated activities of Salmonella type 3 secreted effectors and demonstrates the utility of BioID as a powerful, complementary tool to characterize effector-host protein interactions.Show less >
Language :
Anglais
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
INSERM
Université de Lille
Collections :
  • Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Submission date :
2022-06-15T13:57:47Z
Université de Lille

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