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

Acta Biologica Hungarica
J E KerriganNarayanan Ramasubbu

Abstract

Bacteria in a biofilm are enmeshed in a self-synthesized extracellular polysaccharide matrix (PGA), which is a linear polymer of beta(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 alpha/beta TIM-barrel protein and belongs to family 20 glycosyl hydrolases members. The enzyme activity of DspB with regard to its substrate specificity towards beta(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 beta(1,6)-linked GlcNAc oligosaccharide bound to the active site better that beta(1,4)-linked GlcNAc oligosaccharide. Our combined results indicate that DspB is an exo-acting enzyme that hydrolyzes beta(1,6)-linked N-acetylglucosamine oligomers.

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Citations

Oct 26, 2010·Animal Health Research Reviews·Mario JacquesYannick D N Tremblay
Sep 10, 2009·Veterinary Research·Josée LabrieMario Jacques
Aug 15, 2020·Scientific Reports·Scott MazurkewichJohan Larsbrink
Mar 12, 2020·ACS Infectious Diseases·Declan Alan Gray, Michaela Wenzel
Jan 10, 2020·ACS Chemical Biology·Alexander EddendenMark Nitz

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