title: Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms.
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.
authors.affiliation: Department of Microbiology and Immunology, Emory University School of Medicine, 3105 Rollins Research Center, 1510 Clifton Rd. N.E., Atlanta, GA 30322, USA.
authors.forename: Yoshikane
authors.initials: Y
authors.lastname: Itoh
authors.forename: Xin
authors.initials: X
authors.lastname: Wang
authors.forename: B Joseph
authors.initials: BJ
authors.lastname: Hinnebusch
authors.forename: James F
authors.initials: JF
authors.lastname: Preston
authors.forename: Tony
authors.initials: T
authors.lastname: Romeo
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D016976:Aggregatibacter actinomycetemcomitans / Q000201:enzymology*; D001422:Bacterial Adhesion; D018441:Biofilms; D009876:Operon; D001619:beta-N-Acetylhexosaminidases / Q000502:physiology*
chemical_list: D001619:beta-N-Acetylhexosaminidases; D000117:Acetylglucosamine