A special feature of the bacterium Streptococcus pyogenes enables spontaneous amide bond formation within its surface proteins. We re-engineered this system to generate an irreversible peptide-protein interaction (SpyTag/SpyCatcher). This reaction is genetically-encodable, specific in diverse biological environments, and occurs at a rate close to the diffusion limit. Latest advances include a toolbox of modules for rapidly controlling protein architectures and interaction switchable by temperature, pH or light. We have also developed another bacterial superglue called NeissLock for covalent reaction to endogenous human proteins via an anhydride. For targeting in the GI tract, we have been engineering plant-based proteins with extreme resilience to low pH and proteases. Applications of the technologies will be discussed for hydrogen-deuterium exchange, cell therapy and vaccination, including for emerging pandemic threats.
X/Twitter account – @HowarthSci
- Speaker: Professor Mark Howarth, University of Cambridge
- Monday 04 December 2023, 11:00-12:00
- Venue: In person in the Max Perutz Lecture Theatre (CB2 0QH) and via Zoom, link: https://mrc-lmb-cam-ac-uk.zoom.us/j/95625236862?pwd=NGttT1d6ay9SWFRqUHMvRWNPdDhyZz09.
- Series: MRC LMB Seminar Series; organiser: Scientific Meetings Co-ordinator.