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

被引：233

作者：

Itoh, Y

Wang, X

Hinnebusch, BJ

Preston, JF

Romeo, T

机构：

[1] Emory Univ, Sch Med, Dept Microbiol & Immunol, Rollins Res Ctr 3105, Atlanta, GA 30322 USA

[2] NIAID, Lab Human Bacterial Pathogenesis, Rocky Mt Labs, NIH, Hamilton, MT USA

[3] Univ Florida, Dept Microbiol & Cell Sci, Gainesville, FL 32611 USA

来源：

JOURNAL OF BACTERIOLOGY | 2005年 / 187卷 / 01期

关键词：

D O I：

10.1128/JB.187.1.382-387.2005

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

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页码：382 / 387

页数：6

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