Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus

Lambert, Carey and Cadby, Ian and Till, Rob and Bui, Nhat Khai and Lerner, Thomas R. and Hughes, William S. and Lee, David J. and Alderwick, Luke J. and Vollmer, Waldemar and Sockett, R. Elizabeth and Lovering, Andrew L. (2015) Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus. Nature Communications, 6 . p. 8884. ISSN 2041-1723

[img]
Preview
PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
Available under Licence Creative Commons Attribution.
Download (2MB) | Preview

Abstract

Predatory Bdellovibrio bacteriovorus are natural antimicrobial organisms, killing other bacteria by whole-cell invasion. Self-protection against prey-metabolizing enzymes is important for the evolution of predation. Initial prey entry involves the predator’s peptidoglycan DD-endopeptidases, which decrosslink cell walls and prevent wasteful entry by a second predator. Here we identify and characterize a self-protection protein from B. bacteriovorus, Bd3460, which displays an ankyrin-based fold common to intracellular pathogens of eukaryotes. Co-crystal structures reveal Bd3460 complexation of dual targets, binding a conserved epitope of each of the Bd3459 and Bd0816 endopeptidases. Complexation inhibits endopeptidase activity and cell wall decrosslinking in vitro. Self-protection is vital — DBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morpholog, and lose predatory capacity and cellular integrity. Our analysis provides the first mechanistic examination of self-protection in Bdellovibrio, documents protection-multiplicity for products of two different genomic loci, and reveals an important evolutionary adaptation to an invasive predatory bacterial lifestyle.

Item Type: Article
Keywords: Bacterial evolution, Cell invasion, Membrane proteins, Protein folding
Schools/Departments: University of Nottingham, UK > Faculty of Medicine and Health Sciences > School of Life Sciences
Identification Number: https://doi.org/10.1038/ncomms9884
Depositing User: Sockett, Liz
Date Deposited: 04 Jan 2017 11:42
Last Modified: 04 Jan 2017 11:44
URI: http://eprints.nottingham.ac.uk/id/eprint/39558

Actions (Archive Staff Only)

Edit View Edit View