Broad-spectrum biofilm inhibition by Kingella kingae exopolysaccharide

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Journal titleJournal of Bacteriology
Pages38793886; # of pages: 8
Subjectexopolysaccharide; galactan; galactofuranosyl transferase; mutase; transferase; UDP galactopyranose mutase; unclassified drug; Actinobacillus pleuropneumoniae; Aggregatibacter actinomycetemcomitans; article; biofilm; Candida albicans; carbohydrate analysis; carbohydrate synthesis; cell surface; chemical analysis; controlled study; Escherichia coli; gene cluster; inhibition kinetics; Kingella kingae; Klebsiella pneumoniae; nonhuman; priority journal; Staphylococcus aureus; Staphylococcus epidermidis; Bacterial Physiological Phenomena; Bacterial Proteins; Biofilms; Down-Regulation; Fungi; Kingella kingae; Molecular Sequence Data; Polysaccharides, Bacterial; Actinobacillus pleuropneumoniae serovar 5; Bacteria (microorganisms); Candida albicans; Escherichia coli; Kingella kingae; Klebsiella pneumoniae; Staphylococcus aureus; Staphylococcus epidermidis
AbstractCell-free extracts prepared from Kingella kingae colony biofilms were found to inhibit biofilm formation by Aggregatibacter actinomycetemcomitans, Klebsiella pneumoniae, Staphylococcus aureus, Staphylococcus epidermidis, Candida albicans, and K. kingae. The extracts evidently inhibited biofilm formation by modifying the physicochemical properties of the cell surface, the biofilm matrix, and the substrate. Chemical and biochemical analyses indicated that the biofilm inhibition activity in the K. kingae extract was due to polysaccharide. Structural analyses showed that the extract contained two major polysaccharides. One was a linear polysaccharide with the structure →6)-α-D-GlcNAcp-(1→5)-β-D-OclAp-(2→, which was identical to a capsular polysaccharide produced by Actinobacillus pleuropneumoniae serotype 5. The second was a novel linear polysaccharide, designated PAM galactan, with the structure →3)-β-D-Galf-(1→6)-β-D-Galf-(1→. Purified PAM galactan exhibited broad-spectrum biofilm inhibition activity. A cluster of three K. kingae genes encoding UDP-galactopyranose mutase (ugm) and two putative galactofuranosyl transferases was sufficient for the synthesis of PAM galactan in Escherichia coli. PAM galactan is one of a growing number of bacterial polysaccharides that exhibit antibiofilm activity. The biological roles and potential technological applications of these molecules remain unknown. © 2011, American Society for Microbiology.
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AffiliationNational Research Council Canada (NRC-CNRC)
Peer reviewedYes
NPARC number21271628
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Record identifier93f29cca-f8a9-4c7d-986f-76739a56e66c
Record created2014-03-24
Record modified2016-05-09
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