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Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion Proteins

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 427, Issue 23, Pages 3754-3765

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2015.09.010

Keywords

biofilms; self/non-self recognition; toxin/immunity proteins; type V secretion

Funding

  1. National Institutes of Health [U01 GM102318]
  2. National Science Foundation [DGE-1144085]
  3. Tr-Counties Blood Bank Postdoctoral Fellowship

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Bacteria have developed several strategies to communicate and compete with one another in complex environments. One important mechanism of inter-bacterial competition is contact-dependent growth inhibition (CDI), in which Gram-negative bacteria use CdiB/CdiA two-partner secretion proteins to suppress the growth of neighboring target cells. CdiB is an Omp85 outer-membrane protein that exports and assembles CdiA exoproteins onto the inhibitor cell surface. CdiA binds to receptors on susceptible bacteria and subsequently delivers its C-terminal toxin domain (CdiA-CT) into the target cell. CDI systems also encode Cdil immunity proteins, which specifically bind to the CdiA-CT and neutralize its toxin activity, thereby protecting CUI+ cells from auto-inhibition. Remarkably, CdiA-CT sequences are highly variable between bacteria, as are the corresponding Cdil immunity proteins. Variations in CDI toxin/immunity proteins suggest that these systems function in bacterial self/non-self recognition and thereby play an important role in microbial communities. In this review, we discuss recent advances in the biochemistry, structural biology and physiology of CDI. (C) 2015 Elsevier Ltd. All rights reserved.

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