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Acd, a peptidoglycan hydrolase of Clostridium difficile with N-acetylglucosaminidase activity.
- Source :
-
Microbiology (Reading, England) [Microbiology (Reading)] 2005 Jul; Vol. 151 (Pt 7), pp. 2343-2351. - Publication Year :
- 2005
-
Abstract
- A gene encoding a putative peptidoglycan hydrolase was identified by sequence similarity searching in the Clostridium difficile 630 genome sequence, and the corresponding protein, named Acd (autolysin of C. difficile) was expressed in Escherichia coli. The deduced amino acid sequence of Acd shows a modular structure with two main domains: an N-terminal domain exhibiting repeated sequences and a C-terminal catalytic domain. The C-terminal domain exhibits sequence similarity with the glucosaminidase domains of Staphylococcus aureus Atl and Bacillus subtilis LytD autolysins. Purified recombinant Acd produced in E. coli was confirmed to be a cell-wall hydrolase with lytic activity on the peptidoglycan of several Gram-positive bacteria, including C. difficile. The hydrolytic specificity of Acd was studied by RP-HPLC analysis and MALDI-TOF MS using B. subtilis cell-wall extracts. Muropeptides generated by Acd hydrolysis demonstrated that Acd hydrolyses peptidoglycan bonds between N-acetylglucosamine and N-acetylmuramic acid, confirming that Acd is an N-acetylglucosaminidase. The transcription of the acd gene increased during vegetative cellular growth of C. difficile 630. The sequence of the acd gene appears highly conserved in C. difficile strains. Regarding deduced amino acid sequences, the C-terminal domain with enzymic function appears to be the most conserved of the two main domains. Acd is the first known autolysin involved in peptidoglycan hydrolysis of C. difficile.
- Subjects :
- Acetylglucosaminidase chemistry
Acetylglucosaminidase genetics
Bacterial Proteins biosynthesis
Bacterial Proteins isolation & purification
Bacteriolysis
Clostridioides difficile genetics
Clostridioides difficile physiology
Genome, Bacterial
Hydrolases chemistry
Molecular Sequence Data
Peptidoglycan metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Acetylglucosaminidase metabolism
Bacterial Proteins genetics
Clostridioides difficile enzymology
Hydrolases metabolism
N-Acetylmuramoyl-L-alanine Amidase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1350-0872
- Volume :
- 151
- Issue :
- Pt 7
- Database :
- MEDLINE
- Journal :
- Microbiology (Reading, England)
- Publication Type :
- Academic Journal
- Accession number :
- 16000724
- Full Text :
- https://doi.org/10.1099/mic.0.27878-0