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Journal of Bacteriology, December 2004, p. 8213-8220, Vol. 186, No. 24
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.24.8213-8220.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Genes Involved in the Synthesis and Degradation of Matrix Polysaccharide in Actinobacillus actinomycetemcomitans and Actinobacillus pleuropneumoniae Biofilms

Jeffrey B. Kaplan,1* Kabilan Velliyagounder,1 Chandran Ragunath,1 Holger Rohde,2 Dietrich Mack,2 Johannes K.-M. Knobloch,2 and Narayanan Ramasubbu1

Department of Oral Biology, New Jersey Dental School, Newark, New Jersey,1 Institut für Infektionsmedizin, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany2

Received 7 May 2004/ Accepted 7 September 2004

Biofilms are composed of bacterial cells embedded in an extracellular polysaccharide matrix. A major component of the Escherichia coli biofilm matrix is PGA, a linear polymer of N-acetyl-D-glucosamine residues in ß(1,6) linkage. PGA mediates intercellular adhesion and attachment of cells to abiotic surfaces. In this report, we present genetic and biochemical evidence that PGA is also a major matrix component of biofilms produced by the human periodontopathogen Actinobacillus actinomycetemcomitans and the porcine respiratory pathogen Actinobacillus pleuropneumoniae. We also show that PGA is a substrate for dispersin B, a biofilm-releasing glycosyl hydrolase produced by A. actinomycetemcomitans, and that an orthologous dispersin B enzyme is produced by A. pleuropneumoniae. We further show that A. actinomycetemcomitans PGA cross-reacts with antiserum raised against polysaccharide intercellular adhesin, a staphylococcal biofilm matrix polysaccharide that is genetically and structurally related to PGA. Our findings confirm that PGA functions as a biofilm matrix polysaccharide in phylogenetically diverse bacterial species and suggest that PGA may play a role in intercellular adhesion and cellular detachment and dispersal in A. actinomycetemcomitans and A. pleuropneumoniae biofilms.

* Corresponding author. Mailing address: Medical Science Building, Room C-636, 185 S. Orange Ave., Newark, NJ 07103. Phone: (973) 972-9508. Fax: (973) 972-0045. E-mail: kaplanjb{at}umdnj.edu.

Journal of Bacteriology, December 2004, p. 8213-8220, Vol. 186, No. 24
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.24.8213-8220.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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