Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae

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TypeArticle
Journal titleMicrob.Pathog.
Volume43
Issue1
Pages19; # of pages: 9
SubjectActinobacillus; Actinobacillus pleuropneumoniae; Adhesins,Bacterial; Ampicillin; Anti-Bacterial Agents; bacterial; Bacterial Proteins; Biofilms; CHAIN; CHAINS; chemical; chemistry; Chromosomes,Bacterial; drug effects; Drug Resistance; ENZYME; Escherichia; Escherichia coli; ESCHERICHIA-COLI; FIELD; Form; Galactans; GENE; Gene Deletion; genetics; GlcNAc; Glycosyltransferases; growth & development; In Vitro; isolation & purification; linear; Magnetic Resonance Spectroscopy; matrix; metabolism; Molecular Sequence Data; MUTANT; NMR; NMR spectroscopy; NMR-spectroscopy; PATHOGENESIS; pharmacology; physiology; PIGS; Pleuropneumoniae; Polymerase Chain Reaction; POLYSACCHARIDE; Polysaccharides; Polysaccharides,Bacterial; RESIDUES; SEROTYPE; SEROTYPES; SPECTROSCOPY; Staphylococcus aureus; STRAIN; STRAINS; structure; surface; Swine; transferase
AbstractMost field isolates of the swine pathogen Actinobacillus pleuropneumoniae form tenacious biofilms on abiotic surfaces in vitro. We purified matrix polysaccharides from biofilms produced by A. pleuropneumoniae field isolates IA1 and IA5 (serotypes 1 and 5, respectively), and determined their chemical structures by using NMR spectroscopy. Both strains produced matrix polysaccharides consisting of linear chains of N-acetyl-D-glucosamine (GlcNAc) residues in beta(1,6) linkage (poly-beta-1,6-GlcNAc or PGA). A small percentage of the GlcNAc residues in each polysaccharide were N-deacetylated. These structures were nearly identical to those of biofilm matrix polysaccharides produced by Escherichia coli, Staphylococcus aureus and Staphylococcus epidermidis. PCR analyses indicated that a gene encoding the PGA-specific glycoside transferase enzyme PgaC was present on the chromosome of 15 out of 15 A. pleuropneumoniae reference strains (serotypes 1-12) and 76 out of 77 A. pleuropneumoniae field isolates (serotypes 1, 5 and 7). A pgaC mutant of strain IA5 failed to form biofilms in vitro, as did wild-type strains IA1 and IA5 when grown in broth supplemented with the PGA-hydrolyzing enzyme dispersin B. Treatment of IA5 biofilms with dispersin B rendered them more sensitive to killing by ampicillin. Our findings suggest that PGA functions as a major biofilm adhesin in A. pleuropneumoniae. Biofilm formation may have relevance to the colonization and pathogenesis of A. pleuropneumoniae in pigs
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberIZANO2007
NPARC number9388937
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Record identifier90e6da81-23ef-4159-b563-88a592f77d19
Record created2009-07-10
Record modified2016-05-09
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