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

Lambert, Carey and Cadby, Ian T 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 Sockett, Elizabeth R and Lovering, Andrew L (2015) Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus. Nature Communications, 6. ISSN 2041-1723

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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 - ΔBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morphology, 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
Identification Number: https://doi.org/10.1038/ncomms9884
Date: 2 December 2015
Uncontrolled Keywords: Bacterial evolution, Cell invasion, Membrane proteins, Protein folding
Subjects: C100 Biology
C500 Microbiology
Divisions: Faculty of Health, Education and Life Sciences > School of Health Sciences
Depositing User: David Lee
Date Deposited: 14 Jan 2020 08:49
Last Modified: 12 Feb 2020 13:13
URI: http://www.open-access.bcu.ac.uk/id/eprint/8711

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