Depolymerization of β-1,6- N -Acetyl- d -Glucosamine Disrupts the Integrity of Diverse Bacterial Biofilms-Reference-Cited by-同舟云学术

Depolymerization of β-1,6- N -Acetyl- d -Glucosamine Disrupts the Integrity of Diverse Bacterial Biofilms

Published:2005-01 Issue:1 Volume:187 Page:382-387
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Itoh Yoshikane¹,Wang Xin¹,Hinnebusch B. Joseph²,Preston James F.³,Romeo Tony¹

Affiliation:

1. Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia

2. Laboratory of Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana

3. Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida

Abstract

ABSTRACT Polymeric β-1,6- N -acetyl- d -glucosamine (poly-β-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-β-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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.187.1.382-387.2005

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