Modeling and biochemical analysis of the activity of antibiofilm agent Dispersin B

J. E. Kerrigan, C. Ragunath, Lili Kandra, Gyöngyi Gyémánt, A. Lipták, L. Jánossy, J. B. Kaplan, N. Ramasubbu

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Bacteria in a biofilm are enmeshed in a self-synthesized extracellular polysaccharide matrix (PGA), which is a linear polymer of β(1,6)-linked N-acetylglucosamine (GlcNAc) residues. Dispersin B (DspB), a soluble glycoside hydrolase produced by the periodontal pathogen Actinobacillus actinomycetemcomitans degrades PGA. The enzyme DspB is an α/β TIM-barrel protein and belongs to family 20 glycosyl hydrolases members. The enzyme activity of DspB with regard to its substrate specificity towards β(1,6)-linked GlcNAc polymers and its endo/exo character was investigated through ligand docking and the hydrolysis of synthetic oligosaccharides. Ligand docking analysis suggested that β(1,6)-linked GlcNAc oligosaccharide bound to the active site better that β(1,4)-linked GlcNAc oligosaccharide. Our combined results indicate that DspB is an exo-acting enzyme that hydrolyzes β(1,6)-linked N-acetylglucosamine oligomers.

Original languageAmerican English
Pages (from-to)439-451
Number of pages13
JournalActa Biologica Hungarica
Volume59
Issue number4
DOIs
StatePublished - Dec 2008

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology
  • General Environmental Science
  • Neurology

Keywords

  • Biofilm
  • Dispersin B
  • Exo-acting
  • HPLC
  • Hydrolysis
  • Molecular modeling

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