Phage-neutralizing antibody

The affinity of antibodies selected from naive, synthetic, or even immune phage libraries is typically sufficient for use as a research reagent, but too low for some specific therapeutic applications such as viral neutralization or tumor imaging. For many applications, affinity maturation can be bypassed completely by the construction of multivalent molecules. If this is not sufficient selected antibody clones may be affinity matured (see Figure 18.13). 

Ames RS, Tornetta MA, Jones CS, Tsui P, Isolation of neutralizing anti-C5a monoclonal antibodies from a filamentous phage monovalent Fab display library, J. Immunol., 152 4572-4581, 1994. 

RS Ames, MA Tometta, LJ McMillan. Neutralizing murine monoclonal antibodies to human IL-5 isolated from hybridomas and a filamentous phage Fab display library. J Immunol 1545 6355-6364, 1995. 

After a protein target is functionally validated by CALI, antibodies can be generated using phage display and screened for antibodies that are neutralizing, thereby circumventing structural proteomic approaches. This... 

P22 phage antibody neutralizes phage activity more efficiently than transducing activity. This is also true for inactivation by ultraviolet irradiation. 

Neutralizing anti-phage antibodies have been reported in phage therapy trials in humans (Kucharewicz-Krukowska Slopek, 1987) and animals... 

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