Hosted by Cardiff University's School of Medicine
Abstract: 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. Applications of the technologies will be discussed for hydrogen-deuterium exchange, cell therapy and vaccination, including for emerging pandemic threats
Biography: Mark Howarth is the Sheild Professor in Cambridge University Department of Pharmacology. He co-founded the company SpyBiotech and has been awarded the Royal Society of Chemistry Norman Heatley Award. He did postdoctoral studies at MIT with Alice Ting, where he developed monovalent streptavidin and single molecule probes for tracking neurotransmitter receptors. His doctoral work was with Tim Elliott at Southampton University on MHC class I-peptide quality control. His current work is on innovating ultra-stable protein interactions through peptide superglues, NeissLock and gastrobodies. These tools are being applied to vaccine development, cell therapy and cancer targeting.
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