Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms.
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.
Itoh
Yoshikane
Y
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
X
Hinnebusch
B Joseph
BJ
Preston
James F
JF
Romeo
Tony
T
D000117:Acetylglucosamine / Q000378:metabolism*; D016976:Aggregatibacter actinomycetemcomitans / Q000201:enzymology*; D001422:Bacterial Adhesion; D018441:Biofilms; D009876:Operon; D001619:beta-N-Acetylhexosaminidases / Q000502:physiology*
D001619:beta-N-Acetylhexosaminidases; D000117:Acetylglucosamine