Unbiased Proteomic Profiling Strategy for Discovery of Bacterial Effector Proteins Reveals that Salmonella Protein PheA Is a Host Cell Cycle Regulator. Issue 4 (23rd April 2015)

• Record Type: Journal Article
• Authors: Na, Ha-Na; Yoo, Young-Hwa; Yoon, Chang No; Lee, Jun-Seok
• Is Part Of: Chemistry & biology. Volume 22:Issue 4(2015)
• Page Start: 453
• Page End: 459
• Publication Date: 2015-04-23
• Subjects: Biochemistry -- Periodicals; 540
• DOI: 10.1016/j.chembiol.2015.03.008
• Languages: English
• ISSNs: 1074-5521

Abstract

<abstract abstract-type="author" id="abs0010"> <title id="sectitle0010">Summary</title> <sec> <p id="abspara0010"> <italic>Salmonella</italic> utilizes a type III secretion system to inject bacterial effector proteins into the host cell cytosol. Once in the cytosol, these effectors hijack various biochemical pathways to regulate virulence. Despite the importance of effector proteins, especially for understanding host-pathogen interactions, a potentially large number of effectors are yet to be identified. Here, we demonstrate that unbiased chemical proteomic profiling using off-the-shelf fluorescent probes leads to the discovery of a host cell cycle regulator encoded in the <italic>Salmonella</italic> genome. Our profiling combined with bioinformatic analysis implicates 29 <italic>Salmonella</italic> as potential effectors. We follow up on the top candidate, chorismate mutase-P/prehenate dehydratase, PheA, and present evidence that PheA is an effector that mimics E2F7 transcription factor of the host cell and promotes G1/S cell cycle arrest. This validates our strategy and opens opportunities for effector identification in the future.</p> </sec> </abstract>