A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria

Stephanie K. Aoki, Elie J. Diner, Claire t’Kint de Roodenbeke, Brandt R. Burgess, Stephen J. Poole, Bruce A. Braaten, Allison M. Jones, Julia S. Webb, Christopher S. Hayes, Peggy A. Cotter and David A. Low ()
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Stephanie K. Aoki: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Elie J. Diner: Biomolecular Science and Engineering Program, University of California – Santa Barbara (UCSB)
Claire t’Kint de Roodenbeke: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Brandt R. Burgess: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Stephen J. Poole: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Bruce A. Braaten: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Allison M. Jones: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Julia S. Webb: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Christopher S. Hayes: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
Peggy A. Cotter: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)
David A. Low: Cellular, and Developmental Biology, University of California – Santa Barbara (UCSB)

Nature, 2010, vol. 468, issue 7322, 439-442

Abstract: Contact toxins in bacteria Contact-dependent growth inhibition (CDI), first described in Escherichia coli five years ago, is a mechanism by which cell-to-cell contact inhibits the growth of bacterial cells that do not have this system. CDI is mediated by the two-partner secretion proteins CdiA and CdiB, and a small immunity protein CdiI gives protection against autoinhibition. The molecular basis for some of the interactions involved in CDI has now been elucidated; the toxic properties of CdiA are contained within the protein's carboxy-terminal end (CdiA-CT). A search across other E. coli strains and bacterial species shows the system to be widespread — a range of bacteria contain one or more CdiA homologues, with varied CdiA-CT toxin sequences. These findings suggest that CDI systems constitute an intricate immunity network with an important function in bacterial growth competition in the environment.

Date: 2010
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DOI: 10.1038/nature09490

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