Premium
The F pilus mediates a novel pathway of CDI toxin import
Author(s) -
Beck Christina M.,
Diner Elie J.,
Kim Jeff J.,
Low David A.,
Hayes Christopher S.
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12658
Subject(s) - pilus , pilin , biology , toxin , fimbriae proteins , escherichia coli , colicin , microbiology and biotechnology , effector , bacteria , biochemistry , gene , genetics
Summary Contact‐dependent growth inhibition ( CDI ) is a widespread form of inter‐bacterial competition that requires direct cell‐to‐cell contact. CDI + inhibitor cells express CdiA effector proteins on their surface. CdiA binds to specific receptors on susceptible target bacteria and delivers a toxin derived from its C ‐terminal region ( CdiA ‐ CT ). Here, we show that purified CdiA ‐ CT 536 toxin from uropathogenic E scherichia coli 536 translocates into bacteria, thereby by‐passing the requirement for cell‐to‐cell contact during toxin delivery. Genetic analyses demonstrate that the N ‐terminal domain of CdiA ‐ CT 536 is necessary and sufficient for toxin import. The CdiA receptor plays no role in this import pathway; nor do the Tol and Ton systems, which are exploited to internalize colicin toxins. Instead, CdiA ‐ CT 536 import requires conjugative F pili. We provide evidence that the N ‐terminal domain of CdiA ‐ CT 536 interacts with F pilin, and that pilus retraction is critical for toxin import. This pathway is reminiscent of the strategy used by small RNA leviviruses to infect F + cells. We propose that CdiA ‐ CT 536 mimics the pilin‐binding maturation proteins of leviviruses, allowing the toxin to bind F pili and become internalized during pilus retraction.