Modeling and biochemical analysis of the activity of antibiofilm agent Dispersin B.
Modeling and biochemical analysis of the activity of antibiofilm agent Dispersin B.
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DOI：
10.1556/abiol.59.2008.4.5
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发表时间：
2008-12
影响因子：
--
通讯作者：
Ramasubbu N
中科院分区：
文献类型：
--
作者：
Kerrigan JE;Ragunath C;Kandra L;Gyémánt G;Lipták A;Jánossy L;Kaplan JB;Ramasubbu N
生物膜中的细菌被自身合成的胞外多糖基质（PGA）所包围，所述胞外多糖基质是β（1，6）-连接的N-乙酰葡糖胺（GlcNAc）残基的线性聚合物。分散素B（Dispersin B，Dsp B）是牙周致病菌伴放线杆菌（Actinobacillusactinomycetemcomitans）产生的一种可溶性糖苷水解酶，可降解PGA。DspB是一种α/β TIM桶蛋白，属于20糖基水解酶家族成员。通过配体对接和合成寡糖的水解研究了DspB的酶活性，包括其对β（1，6）-连接的GlcNAc聚合物的底物特异性及其内/外特性。配体对接分析表明，β（1，6）-连接的GlcNAc寡糖比β（1，4）-连接的GlcNAc寡糖更好地结合到活性位点上。我们的综合结果表明，DspB是一种水解β（1，6）-连接的N-乙酰葡糖胺寡聚体的外切作用酶。
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.