This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hayashi, H. Articles by Ito, E. Search for Related Content PubMed PubMed Citation Articles by Hayashi, H. Articles by Ito, E.

Occurrence of Glucosamine Residues with Free Amino Groups in Cell Wall Peptidoglycan from Bacilli as a Factor Responsible for Resistance to Lysozyme

Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, Japan

ABSTRACT

Analysis by dinitrophenylation techniques revealed the occurrence of significant amounts of glucosamine residues with free amino groups in the peptidoglycan component of cell walls isolated from Bacillus cereus, Bacillus subtilis, and Bacillus megaterium. A close correlation was demonstrated between the content of N-unacetylated glucosamine residues in the peptidoglycan component and the resistance of the cell walls to lysozyme. These lysozyme-resistant cell walls and peptidoglycan were converted into a lysozyme-sensitive form by means of N-acetylation with acetic anhydride. Thus, the occurrence of the N-unacetylated glucosamine residues in the peptidoglycan component accounts for the resistance of these cell walls to lysozyme. The N-unacetylated glucosamine residues were not found in a significant amount in the cell walls of Micrococcus lysodeikticus, Staphylococcus aureus, Streptococcus faecalis, Lactobacillus casei, or Lactobacillus arabinosus.

This article has been cited by other articles:

• Meyrand, M., Boughammoura, A., Courtin, P., Mezange, C., Guillot, A., Chapot-Chartier, M.-P. (2007). Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis. Microbiology 153: 3275-3285 [Abstract] [Full Text]  
• Marraffini, L. A., Schneewind, O. (2007). Sortase C-Mediated Anchoring of BasI to the Cell Wall Envelope of Bacillus anthracis. J. Bacteriol. 189: 6425-6436 [Abstract] [Full Text]  
• Zawadzka-Skomial, J., Markiewicz, Z., Nguyen-Disteche, M., Devreese, B., Frere, J.-M., Terrak, M. (2006). Characterization of the Bifunctional Glycosyltransferase/Acyltransferase Penicillin-Binding Protein 4 of Listeria monocytogenes.. J. Bacteriol. 188: 1875-1881 [Abstract] [Full Text]  
• Mahapatra, S., Yagi, T., Belisle, J. T., Espinosa, B. J., Hill, P. J., McNeil, M. R., Brennan, P. J., Crick, D. C. (2005). Mycobacterial Lipid II Is Composed of a Complex Mixture of Modified Muramyl and Peptide Moieties Linked to Decaprenyl Phosphate. J. Bacteriol. 187: 2747-2757 [Abstract] [Full Text]  
• Beukes, M., Hastings, J. W. (2001). Self-Protection against Cell Wall Hydrolysis in Streptococcus milleri NMSCC 061 and Analysis of the Millericin B Operon. Appl. Environ. Microbiol. 67: 3888-3896 [Abstract] [Full Text]  
• Beukes, M., Bierbaum, G., Sahl, H.-G., Hastings, J. W. (2000). Purification and Partial Characterization of a Murein Hydrolase, Millericin B, Produced by Streptococcus milleri NMSCC 061. Appl. Environ. Microbiol. 66: 23-28 [Abstract] [Full Text]  
• Vollmer, W., Tomasz, A. (2000). The pgdA Gene Encodes for a Peptidoglycan N-Acetylglucosamine Deacetylase in Streptococcus pneumoniae. J. Biol. Chem. 275: 20496-20501 [Abstract] [Full Text]