Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms.

J Bacteriol

Department of Microbiology and Immunology, Emory University School of Medicine, 3105 Rollins Research Center, 1510 Clifton Rd. N.E., Atlanta, GA 30322, USA.

Published: January 2005

Polymeric beta-1,6-N-acetyl-D-glucosamine (poly-beta-1,6-GlcNAc) has been implicated as an Escherichia coli and Staphylococcus epidermidis biofilm adhesin, the formation of which requires the pgaABCD and icaABCD loci, respectively. Enzymatic hydrolysis of poly-beta-1,6-GlcNAc, demonstrated for the first time by chromatography and mass spectrometry, disrupts biofilm formation by these species and by Yersinia pestis and Pseudomonas fluorescens, which possess pgaABCD homologues.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC538831PMC
http://dx.doi.org/10.1128/JB.187.1.382-387.2005DOI Listing

Publication Analysis

Top Keywords

depolymerization beta-16-n-acetyl-d-glucosamine
4
beta-16-n-acetyl-d-glucosamine disrupts
4
disrupts integrity
4
integrity diverse
4
diverse bacterial
4
bacterial biofilms
4
biofilms polymeric
4
polymeric beta-16-n-acetyl-d-glucosamine
4
beta-16-n-acetyl-d-glucosamine poly-beta-16-glcnac
4
poly-beta-16-glcnac implicated
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!