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

Lambert, Carey; Cadby, Ian T.; Till, Rob; Bui, Nhat Khai; Lerner, Thomas R.; Hughes, William S.; Lee, David J.; Alderwick, Luke J.; Vollmer, Waldemar; Sockett, R. Elizabeth; Lovering, Andrew L.

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


Authors

Ian T. Cadby

Rob Till

Nhat Khai Bui

Thomas R. Lerner

William S. Hughes

David J. Lee

Luke J. Alderwick

Waldemar Vollmer

Andrew L. Lovering



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-?Bd3460 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.

Citation

Lambert, C., Cadby, I. T., Till, R., Bui, N. K., Lerner, T. R., Hughes, W. S., …Lovering, A. L. (2015). Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus. Nature Communications, 6, Article 8884. https://doi.org/10.1038/ncomms9884

Journal Article Type Article
Acceptance Date Oct 12, 2015
Online Publication Date Dec 2, 2015
Publication Date Dec 2, 2015
Deposit Date Jan 4, 2017
Publicly Available Date Mar 29, 2024
Journal Nature Communications
Electronic ISSN 2041-1723
Publisher Nature Publishing Group
Peer Reviewed Peer Reviewed
Volume 6
Article Number 8884
DOI https://doi.org/10.1038/ncomms9884
Keywords Bacterial evolution, Cell invasion, Membrane proteins, Protein folding
Public URL https://nottingham-repository.worktribe.com/output/770384
Publisher URL http://www.nature.com/articles/ncomms9884

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