Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus
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 de...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
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Nature Publishing Group
2015
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| Online Access: | https://eprints.nottingham.ac.uk/39558/ |
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| author | Lambert, Carey Cadby, Ian 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. |
| author_facet | Lambert, Carey Cadby, Ian 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. |
| author_sort | Lambert, Carey |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | 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 — DBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morpholog, 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. |
| first_indexed | 2025-11-14T19:38:52Z |
| format | Article |
| id | nottingham-39558 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:38:52Z |
| publishDate | 2015 |
| publisher | Nature Publishing Group |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-395582020-05-04T17:28:21Z https://eprints.nottingham.ac.uk/39558/ Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus Lambert, Carey Cadby, Ian 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. 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 — DBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morpholog, 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. Nature Publishing Group 2015-12-02 Article PeerReviewed Lambert, Carey, Cadby, Ian, Till, Rob, Bui, Nhat Khai, Lerner, Thomas R., Hughes, William S., Lee, David J., Alderwick, Luke J., Vollmer, Waldemar, Sockett, R. Elizabeth and Lovering, Andrew L. (2015) Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus. Nature Communications, 6 . p. 8884. ISSN 2041-1723 Bacterial evolution Cell invasion Membrane proteins Protein folding http://www.nature.com/articles/ncomms9884 DOI: 10.1038/ncomms9884 DOI: 10.1038/ncomms9884 |
| spellingShingle | Bacterial evolution Cell invasion Membrane proteins Protein folding Lambert, Carey Cadby, Ian 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 |
| title | Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus |
| title_full | Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus |
| title_fullStr | Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus |
| title_full_unstemmed | Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus |
| title_short | Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus |
| title_sort | ankyrin-mediated self-protection during cell invasion by the bacterial predator bdellovibrio bacteriovorus |
| topic | Bacterial evolution Cell invasion Membrane proteins Protein folding |
| url | https://eprints.nottingham.ac.uk/39558/ https://eprints.nottingham.ac.uk/39558/ https://eprints.nottingham.ac.uk/39558/ |