Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus.
Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus.
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DOI:
10.1038/ncomms9884
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发表时间:
2015-12-02
影响因子:
16.6
通讯作者:
Lovering AL
中科院分区:
文献类型:
--
作者:
Lambert C;Cadby IT;Till R;Bui NK;Lerner TR;Hughes WS;Lee DJ;Alderwick LJ;Vollmer W;Sockett RE;Lovering AL
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. The bacterium Bdellovibrio bacteriovorus invades and kills other bacteria, but it is unclear how it avoids degradation of its own cell wall. Here the authors identify the B. bacteriovorus protein Bd3460 as an endopeptidase inhibitor that prevents hydrolysis of the predator's peptidoglycan during invasion of prey.