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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; Sockett, Elizabeth R; Lovering, Andrew L.
Affiliation
  • Lambert C; Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK.
  • Cadby IT; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
  • Till R; Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK.
  • Bui NK; Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne NE2 4AX, UK.
  • Lerner TR; Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK.
  • Hughes WS; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
  • Lee DJ; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
  • Alderwick LJ; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
  • Vollmer W; Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne NE2 4AX, UK.
  • Sockett RE; Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK.
  • Sockett ER; Centre for Genetics and Genomics, School of Biology, Nottingham University, Medical School, Queen's Medical Centre, Nottingham NG7 2UH, UK.
  • Lovering AL; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
Nat Commun ; 6: 8884, 2015 Dec 02.
Article in En | MEDLINE | ID: mdl-26626559
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Bdellovibrio / Gene Expression Regulation, Bacterial / Ankyrins / Escherichia coli Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2015 Document type: Article Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Bdellovibrio / Gene Expression Regulation, Bacterial / Ankyrins / Escherichia coli Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2015 Document type: Article Country of publication: