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首页> 外文期刊>Biotechnology Progress >Binding Domains of Bacillus Anthracis Phage Endolysins Recognize Cell Culture Age-Related Features on the Bacterial Surface
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Binding Domains of Bacillus Anthracis Phage Endolysins Recognize Cell Culture Age-Related Features on the Bacterial Surface

机译：炭疽杆菌噬菌体溶血素的结合域识别细菌表面上与细胞培养年龄相关的特征

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Bacteriolytic enzymes often possess a C-terminal binding domain that recognizes specific motifs on the bacterial surface and a catalytic domain that cleaves covalent linkages within the cell wall peptidoglycan. PlyPH, one such lytic enzyme of bacteriophage origin, has been reported to be highly effective against Bacillus anthracis, and can kill up to 99.99% of the viable bacteria. The bactericidal activity of this enzyme, however, appears to be strongly dependent on the age of the bacterial culture. Although highly bactericidal against cells in the early exponential phase, the enzyme is substantially less effective against stationary phase cells, thus limiting its application in real-world settings. We hypothesized that the binding domain of PlyPH may differ in affinity to cells in different Bacillus growth stages and may be primarily responsible for the age-restricted activity. We therefore employed an in silico approach to identify phage lysins differing in their specificity for the bacterial cell wall. Specifically we focused our attention on Ply, an enzyme with improved cell wall-binding ability and age-independent bactericidal activity. Although PlyPH and Ply have dissimilar binding domains, their catalytic domains are highly homologous. We characterized the biocatalytic mechanism of Ply by identifying the specific bonds cleaved within the cell wall peptidoglycan. Our results provide an example of the diversity of phage endolysins and the opportunity for these biocatalysts to be used for broad-based protection from bacterial pathogens. (C) 2015 American Institute of Chemical Engineers
机译：溶菌酶通常具有识别细菌表面上特定基序的C末端结合结构域和裂解细胞壁肽聚糖内共价键的催化结构域。据报道，PlyPH是一种来自噬菌体的裂解酶，对炭疽芽孢杆菌具有很高的抗药性，可以杀死多达99.99％的活细菌。然而，该酶的杀菌活性似乎强烈依赖于细菌培养物的年龄。尽管该酶对指数早期的细胞具有高度的杀菌作用，但其对固定相细胞的作用却明显较低，因此限制了其在现实环境中的应用。我们假设PlyPH的结合域可能在不同的芽孢杆菌生长阶段对细胞的亲和力不同，并且可能主要负责年龄限制活动。因此，我们采用计算机方法鉴定噬菌体溶素对细菌细胞壁的特异性不同。具体而言，我们将注意力集中在Ply上，Ply是一种具有改善的细胞壁结合能力和不依赖年龄的杀菌活性的酶。尽管PlyPH和Ply具有不同的结合结构域，但是它们的催化结构域是高度同源的。我们通过确定在细胞壁肽聚糖内裂解的特定键来表征Ply的生物催化机制。我们的结果提供了噬菌体内溶素多样性的例子，以及这些生物催化剂被广泛用于细菌病原体保护的机会。 （C）2015美国化学工程师学会

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