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Journal of Bacteriology, January 2005, p. 382-387, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.382-387.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Depolymerization of ß-1,6-N-Acetyl-D-Glucosamine Disrupts the Integrity of Diverse Bacterial Biofilms{dagger}

Yoshikane Itoh,1 Xin Wang,1 B. Joseph Hinnebusch,2 James F. Preston III,3 and Tony Romeo1*

Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia,1 Laboratory of Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana,2 Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida3

Received 16 July 2004/ Accepted 20 September 2004

Polymeric ß-1,6-N-acetyl-D-glucosamine (poly-ß-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-ß-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.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Emory University School of Medicine, 3105 Rollins Research Center, 1510 Clifton Rd. N.E., Atlanta, GA 30322. Phone: (404) 727-3734. Fax: (404) 727-3659. E-mail: romeo{at}microbio.emory.edu.

{dagger} This paper is Journal Series no. R-10438 of the University of Florida Agriculture Experiment Station.

Journal of Bacteriology, January 2005, p. 382-387, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.382-387.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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