Characterization of a novel lytic protein encoded by the Bacillus cereus E33L gene ampD as a Bacillus anthracis antimicrobial protein

Appl Environ Microbiol. 2012 Apr;78(8):3025-7. doi: 10.1128/AEM.06906-11. Epub 2012 Feb 17.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / metabolism
  • Bacillus anthracis / cytology
  • Bacillus anthracis / drug effects*
  • Bacillus anthracis / physiology*
  • Bacillus cereus / enzymology*
  • Bacillus cereus / genetics*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Bacteriolysis*
  • Colony Count, Microbial
  • Enzyme Stability
  • Microbial Viability / drug effects
  • Microscopy
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry
  • N-Acetylmuramoyl-L-alanine Amidase / genetics*
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism*
  • Protein Stability

Substances

  • Anti-Infective Agents
  • Bacterial Proteins
  • AmpD protein, Bacteria
  • N-Acetylmuramoyl-L-alanine Amidase