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

Kerrigan, J. and Ragunath, C. and Kandra, Lili and Gyémánt, GYöngyi and Lipták, A. and Jánossy, L. and Kaplan, J. and Ramasubbu, N. (2008) Modeling and biochemical analysis of the activity of antibiofilm agent Dispersin B. Acta Biologica Hungarica, 59 (4). pp. 439-451. ISSN 0236-5383

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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.

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