AI Article Synopsis

  • Bacterial pathogens use virulence proteins, called effectors, to manipulate host cell processes by interacting with host proteins, but these interactions are often brief and hard to detect with traditional methods.
  • In this study, researchers compared two methods, proximity-dependent biotin labeling (BioID) and immunoprecipitation with mass spectrometry, to analyze Salmonella's effector proteins involved in altering host cell trafficking.
  • They identified 632 potential interactions with 381 unique human proteins, highlighting the role of the BLOC-2 protein complex in the positioning and stability of Salmonella-containing vacuoles during infection, thus showcasing the effectiveness of BioID for studying these interactions.

Article Abstract

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.

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http://dx.doi.org/10.1038/s41564-019-0580-9DOI Listing

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