Beijing National Lab. for Molecular Sciences, Key Laboratory of Molecular Nanostructures and Nanotechnology, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, P.R. China.
Nanoscale. 2015 Oct 7;7(37):15245-50. doi: 10.1039/c5nr03525b.
The cell wall binding domain (CBD) of bacteriophage lysins can recognize target bacteria with extraordinary specificity through binding to bacterial peptidoglycan, thus it is a promising new probe to identify the corresponding bacterial pathogen. In this work, we used atomic force microscopy (AFM) based single-molecule force spectroscopy to investigate the interaction between the CBD of lysin PlyV12 (PlyV12C) and pathogenic bacterium Staphylococcus aureus (S. aureus). The binding forces of PlyV12C with S. aureus have been measured, and the dissociation process of their binding complex has been characterized. Furthermore, we compared the interactions of PlyV12C-S. aureus and antibody-S. aureus. It is revealed that PlyV12C has a comparable affinity to bacterial peptidoglycans as that of the S. aureus antibody. The results provide new information on the binding properties of lysin CBD with bacterium, and the application of lysin CBD in bacterium detection.
细胞壁结合结构域（CBD）的噬菌体溶菌酶可以通过与细菌肽聚糖结合，特异性识别靶细菌，因此它是一种很有前途的新型探针，可以用于识别相应的细菌病原体。在这项工作中，我们使用原子力显微镜（AFM）单分子力谱技术研究了溶菌酶 PlyV12（PlyV12C）的 CBD 与致病菌金黄色葡萄球菌（S. aureus）之间的相互作用。测量了 PlyV12C 与 S. aureus 的结合力，并对其结合复合物的解离过程进行了表征。此外，我们比较了 PlyV12C-S. aureus 和抗体-S. aureus 的相互作用。结果表明，PlyV12C 与细菌肽聚糖的亲和力与 S. aureus 抗体相当。这些结果为溶菌酶 CBD 与细菌的结合特性以及溶菌酶 CBD 在细菌检测中的应用提供了新的信息。
