SpyTag/SpyCatcher interactions

6 November 2019, 1.00 PM - 6 November 2019, 2.00 PM

Mark Howarth (Oxford University)

Room G13/14 Life Sciences Building

Hosted by the Bristol BioDesign Research Institute

A special feature of the bacterium Streptococcus pyogenes enables spontaneous isopeptide bond formation within its surface proteins. We re-engineered this system to generate an irreversible peptide-protein interaction (SpyTag/SpyCatcher). This reaction is rapid, genetically-encodable and specific in diverse biological environments. Latest advances include accelerated reactivity and a toolbox of modules for rapidly controlling protein architectures. SpyTag and its related superglue SnoopTag allows programmable synthesis of multi-functional teams or biomaterials, to modulate precisely cancer cell signalling. Vaccines are one of the most successful medical interventions and an important frontier for synthetic biology. Virus-like particles (VLPs) are nano-assemblies with many attractive features for vaccination. However, decorating VLPs with target antigens by genetic fusion or chemical modification is often unsuccessful. We demonstrated 100% reaction to SpyCatcher-VLPs after mixing with SpyTag linked to a range of malaria antigens and cancer targets. Spy-VLPs efficiently induced antibody responses after only a single immunization and without adjuvant. Modular and programmable assembly using SpyTag shows promise in accelerating vaccine development against a range of human and veterinary diseases.

Contact information

For further information or to meet with the spekaer contact Aggie Hewitt (agatha.hewitt@bristol.ac.uk). 

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