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 ti...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1999-09, Vol.262 (3), p.801-805
Main Authors: Ramı́rez, E., Mas, J.M., Carbonell, X., Avilés, F.X., Villaverde, A.
Format: Article
Language:English
Subjects:
Bacteriophage P22
Binding Sites, Antibody
Biosensing Techniques
Fab
Glycoside Hydrolases - chemistry
Immunoglobulin Fab Fragments - chemistry
Macromolecular Substances
Models, Molecular
Protein Binding
Protein Conformation
Recombinant Fusion Proteins - chemistry
Viral Tail Proteins - chemistry
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1999.1268