Journal
JOURNAL OF BACTERIOLOGY
Volume 187, Issue 1, Pages 382-387Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.187.1.382-387.2005
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Funding
- NCRR NIH HHS [1S10 RR 14645-01] Funding Source: Medline
- NIGMS NIH HHS [R01 GM066794, GM066794] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [S10RR014645] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [Z01AI000796, ZIAAI000796] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM066794] Funding Source: NIH RePORTER
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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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