phage display;
bacteriophages;
single virus manipulation;
atomic force microscopy;
force spectroscopy;
ANTIGEN-BINDING FORCES;
ENERGY LANDSCAPES;
HUMAN RHINOVIRUS;
LIVE CELLS;
MICROSCOPY;
PHAGE;
RESOLUTION;
NANOWIRES;
MOLECULES;
COMPLEX;
D O I:
10.1021/nn900778t
中图分类号:
O6 [化学];
学科分类号:
070301 [无机化学];
摘要:
A method is described for the site-directed manipulation of single filamentous bacteriophages, by using phage display technology and atomic force microscopy. f1 filamentous bacteriophages were genetically engineered to display His-tags on their pIX tail. Following adsorption on nitrilotriacetate-terminated surfaces, force spectroscopy with tips bearing monoclonal anti-PIII antibodies was used to pull on individual phages via their PIII head. Analysis of the force-extension profiles revealed that upon pulling, the phages are progressively straightened into an extended orientation until rupture of the anti-PIII/PIII complex. The single-virus manipulation technique presented here provides new opportunities for understanding the forces driving cell-virus and material-virus interactions, and for characterizing the binding properties of polypeptide sequences or proteins selected by the phage display technology.