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The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein

Lookup NU author(s): Dr Christopher Johnson, Professor Antonio Molinaro, Professor Jeremy Lakey

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

Colicins are a diverse family of large antibacterial protein toxins, secreted by and active against Escherichia coli and must cross their target cell's outer membrane barrier to kill. To achieve this, most colicins require an abundant porin (e.g. OmpF) plus a low-copy-number, high-affinity, outer membrane protein receptor (e.g. BtuB). Recently, genetic screens have suggested that colicin N (ColN), which has no high-affinity receptor, targets highly abundant lipopolysaccharide (LPS) instead. Here we reveal the details of this interaction and demonstrate that the ColN receptor-binding domain (ColN-R) binds to a specific region of LPS close to the membrane surface. Data from in vitro studies using calorimetry and both liquid- and solid-state NMR reveal the interactions behind the in vivo requirement for a defined oligosaccharide region of LPS. Delipidated LPS (LPSLIPID) shows weaker binding; and thus full affinity requires the lipid component. The site of LPS binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF. ColN is, currently, unique among colicins in requiring LPS and, combined with previous data, this implies that the ColN translocon is distinct from those of other known colicins.


Publication metadata

Author(s): Johnson CL, Ridley H, Marchetti R, Silipo A, Griffin DC, Crawford L, Bonev B, Molinaro A, Lakey JH

Publication type: Article

Publication status: Published

Journal: Molecular Microbiology

Year: 2014

Volume: 92

Issue: 3

Pages: 440-452

Print publication date: 01/05/2014

Online publication date: 28/03/2014

Acceptance date: 27/02/2014

Date deposited: 23/06/2014

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1111/mmi.12568

DOI: 10.1111/mmi.12568


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