Study of the interactions between endolysin and bacterial peptidoglycan on S. aureus by dynamic force spectroscopy.
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.
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. xfang@iccas.ac.cn.
Jianli
J
Liu
Xuejie
X
Zhang
Hang
H
Yang
Jinghe
J
Yuan
Hongping
H
Wei
Junping
J
Yu
Xiaohong
X
Fang
D010450:Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D008853:Microscopy; D010457:Peptidoglycan / Q000737:chemistry* / Q000378:metabolism; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000378:metabolism
D010457:Peptidoglycan; D010450:Endopeptidases; C001143:endolysin