Our lab has designed and characterized a novel 2-dimensional genetic strategy to modulate the degree of decoration of a desired peptide/protein on the surface of phage l via genetic fusion to its major capsid protein, gpD. This was done by combining various permutations of the gpD allele with controllable expression of gpD::X (fusion) during phage assembly. Our studies represent the first method and attempt to measure surface phage fluorescence (eGFP fused to gpD) on a phage by FACS and the highest degree of controllable phage decoration reported to date [Nicastro et al. 2013. Appl Microbiol Biotechnol 97: 7791-7804]. The patent describing this technology can be found here.

Tuneable lytic phage display has been applied to the generation of “superlytic nanoparticles” expressing phage-encoded S. aureus antibacterial lysin on the capsid surface (MS in preparation) as well as to target our immunogenic phage to dendritic cells via capsid fusions, where phage have also been genetically engineered to genomically encode gag-env HIV VLP therapeutic vaccine sequences. By this strategy each phage may serve as a targeted vehicle for delivery of gag-env VLP sequence for expression and VLP production in dendritic cells to generate optimized immune responses against HIV (in process).