title: Interrupting peptidoglycan deacetylation during Bdellovibrio predator-prey interaction prevents ultimate destruction of prey wall, liberating bacterial-ghosts.
abstract: The peptidoglycan wall, located in the periplasm between the inner and outer membranes of the cell envelope in Gram-negative bacteria, maintains cell shape and endows osmotic robustness. Predatory Bdellovibrio bacteria invade the periplasm of other bacterial prey cells, usually crossing the peptidoglycan layer, forming transient structures called bdelloplasts within which the predators replicate. Prey peptidoglycan remains intact for several hours, but is modified and then degraded by escaping predators. Here we show predation is altered by deleting two Bdellovibrio N-acetylglucosamine (GlcNAc) deacetylases, one of which we show to have a unique two domain structure with a novel regulatory"plug". Deleting the deacetylases limits peptidoglycan degradation and rounded prey cell "ghosts" persist after mutant-predator exit. Mutant predators can replicate unusually in the periplasmic region between the peptidoglycan wall and the outer membrane rather than between wall and inner-membrane, yet still obtain nutrients from the prey cytoplasm. Deleting two further genes encoding DacB/PBP4 family proteins, known to decrosslink and round prey peptidoglycan, results in a quadruple mutant Bdellovibrio which leaves prey-shaped ghosts upon predation. The resultant bacterial ghosts contain cytoplasmic membrane within bacteria-shaped peptidoglycan surrounded by outer membrane material which could have promise as "bacterial skeletons" for housing artificial chromosomes.
authors.affiliation: Centre for Genetics and Genomics, School of Life Sciences, University of Nottingham, Medical School, Queen's Medical Centre, Nottingham, NG7 2UH, UK.
authors.forename: Carey
authors.initials: C
authors.lastname: Lambert
authors.affiliation: The Francis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London, NW7 1AA, UK.
authors.forename: Thomas R
authors.initials: TR
authors.lastname: Lerner
authors.affiliation: The Centre for Bacterial Cell Biology, Baddiley Clark Building, Medical School, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
authors.forename: Nhat Khai
authors.initials: NK
authors.lastname: Bui
authors.affiliation: Centre for Genetics and Genomics, School of Life Sciences, University of Nottingham, Medical School, Queen's Medical Centre, Nottingham, NG7 2UH, UK.
authors.forename: Hannah
authors.initials: H
authors.lastname: Somers
authors.affiliation: Department of Life Sciences, Prefectural University of Hiroshima, Shobara, Hiroshima, 727-0023, Japan.
authors.forename: Shin-Ichi
authors.initials: S
authors.lastname: Aizawa
authors.affiliation: School of Biosciences, University of Nottingham, Sutton Bonington, Leicestershire, LE12 5RD, UK.
authors.forename: Susan
authors.initials: S
authors.lastname: Liddell
authors.affiliation: Centre for Genetics and Genomics, School of Life Sciences, University of Nottingham, Medical School, Queen's Medical Centre, Nottingham, NG7 2UH, UK.
authors.forename: Ana
authors.initials: A
authors.lastname: Clark
authors.affiliation: The Centre for Bacterial Cell Biology, Baddiley Clark Building, Medical School, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
authors.forename: Waldemar
authors.initials: W
authors.lastname: Vollmer
authors.affiliation: Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
authors.forename: Andrew L
authors.initials: AL
authors.lastname: Lovering
authors.affiliation: Centre for Genetics and Genomics, School of Life Sciences, University of Nottingham, Medical School, Queen's Medical Centre, Nottingham, NG7 2UH, UK.
authors.forename: R Elizabeth
authors.initials: RE
authors.lastname: Sockett
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001501:Bdellovibrio / Q000502:physiology*; D002473:Cell Wall / Q000378:metabolism*; D022202:Chromosomes, Artificial, Bacterial / Q000235:genetics / Q000378:metabolism; D004261:DNA Replication / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics* / Q000378:metabolism; D000074041:Microorganisms, Genetically-Modified; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism; D019897:Periplasm / Q000378:metabolism; D059748:Proteolysis; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010457:Peptidoglycan; D017351:N-Acetylglucosaminyltransferases; C063057:UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase