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

Author

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  • Carey Lambert

    (Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen’s Medical Centre)

  • Ian T. Cadby

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • Rob Till

    (Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen’s Medical Centre)

  • Nhat Khai Bui

    (Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University)

  • Thomas R. Lerner

    (Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen’s Medical Centre
    Present address: Francis Crick Institute, London NW1 2BE, UK.)

  • William S. Hughes

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • David J. Lee

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • Luke J. Alderwick

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • Waldemar Vollmer

    (Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University)

  • R. Elizabeth Sockett

    (Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen’s Medical Centre)

  • Andrew L. Lovering

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

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.

Suggested Citation

  • Carey Lambert & Ian T. Cadby & Rob Till & Nhat Khai Bui & Thomas R. Lerner & William S. Hughes & David J. Lee & Luke J. Alderwick & Waldemar Vollmer & R. Elizabeth Sockett & Andrew L. Lovering, 2015. "Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9884
    DOI: 10.1038/ncomms9884
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