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

作者：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

来源：Nature Communications, 2015, 6(1): 8884.

DOI：10.1038/ncomms9884

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 -Delta 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.

• 出版日期2015-12