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PMID: 15601723 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Journal of bacteriology ·Vol. 187 ·No. 1 ·2005-01-00 ·Pages 382-7

Itoh Y, Wang X, Hinnebusch BJ, Preston JF, Romeo T

Abstract

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.

MeSH Terms
Acetylglucosamine/metabolism Aggregatibacter actinomycetemcomitans/enzymology Bacterial Adhesion Biofilms Operon beta-N-Acetylhexosaminidases/physiology
Chemicals
beta-N-Acetylhexosaminidases Acetylglucosamine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Itoh Yoshikane
Department of Microbiology and Immunology, Emory University School of Medicine, 3105 Rollins Research Center, 1510 Clifton Rd. N.E., Atlanta, GA 30322, USA.
Wang Xin
Hinnebusch B Joseph
Preston James F
Romeo Tony
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.187.1.382-387.2005
Published
2005-01-00
Pages
382-7
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC538831
Subset
IM
Grants
NIGMS NIH HHS · R01 GM066794 · United States
NCRR NIH HHS · 1S10 RR 14645-01 · United States
NIGMS NIH HHS · GM066794 · United States
External Links
PubMed source DOI: 10.1128/JB.187.1.382-387.2005 PMC Full Text View journal details
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