Detection of molecular interactions by using a new peptide-displaying bacteriophage biosensor.
Foreign peptides fused to the carboxy terminus of P22 tailspike protein are solvent-exposed and highly antigenic when displayed on the surface of infectious virus particles. Binding of an anti-peptide specific Fab antibody fragment enhances the infectivity of chimeric bacteriophage particles in a titre-dependent fashion. Although the precise molecular basis of this enhanced infectivity remains unclear, experimental data and modelling approaches suggest that the antibody binding might restore conformational impairments in the assembled tail protein affecting its activity and performance during infection. These results suggest that in addition to free enzymes, peptide-displaying bacteriophages could be engineered as new biosensors to detect molecular interactions by using natural viral enzymes critical for cell infection.
Ramírez
E
E
Departament de Genètica i Microbiologia, Universitat Autònoma de Barcelona, Barcelona, Bellaterra, 08193, Spain.
Mas
J M
JM
Carbonell
X
X
Avilés
F X
FX
Villaverde
A
A
D017100:Bacteriophage P22; D001666:Binding Sites, Antibody; D015374:Biosensing Techniques; D006026:Glycoside Hydrolases / Q000737:chemistry*; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D017376:Viral Tail Proteins / Q000737:chemistry*
D007140:Immunoglobulin Fab Fragments; D046911:Macromolecular Substances; D011993:Recombinant Fusion Proteins; D017376:Viral Tail Proteins; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage