title: Characterization of a novel lytic protein encoded by the Bacillus cereus E33L gene ampD as a Bacillus anthracis antimicrobial protein.
abstract: Lytic proteins encoded by bacterial genomes have been implicated in cell wall biosynthesis and recycling. The Bacillus cereus E33L ampD gene encodes a putative N-acetylmuramoyl-l-alanine amidase. This gene, expressed in vitro, produced a very stable, highly active lytic protein. Very low concentrations rapidly and efficiently lyse vegetative Bacillus anthracis cells.
authors.affiliation: Biosciences and Biotechnology Division, Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, California, USA.
authors.forename: Feliza A
authors.initials: FA
authors.lastname: Bourguet
authors.forename: Brian E
authors.initials: BE
authors.lastname: Souza
authors.forename: Angela K
authors.initials: AK
authors.lastname: Hinz
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Coleman
authors.forename: Paul J
authors.initials: PJ
authors.lastname: Jackson
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism; D001408:Bacillus anthracis / Q000166:cytology / Q000187:drug effects* / Q000502:physiology*; D001409:Bacillus cereus / Q000201:enzymology* / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001433:Bacteriolysis; D015169:Colony Count, Microbial; D004795:Enzyme Stability; D050296:Microbial Viability / Q000187:drug effects; D008853:Microscopy; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D055550:Protein Stability
chemical_list: D000890:Anti-Infective Agents; D001426:Bacterial Proteins; C062460:AmpD protein, Bacteria; D009238:N-Acetylmuramoyl-L-alanine Amidase