Join CLP for a virtual lecture by Professor of Protein Nanotechnology at University of Oxford, Mark Howarth, at 10:00 am on Friday, March 18. The Zoom link is here.
Bacterial superglues, spontaneous amide bond formation and nano-assemblies to tickle the immune system
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 rapid, genetically-encodable and specific in diverse biological environments. Latest advances include a toolbox of modules for rapidly controlling protein architectures and temperature- or pH-switchable interaction. We have also developed another bacterial superglue called NeissLock for covalent reaction to endogenous human proteins via an anhydride. Applications will be discussed for cell therapy and vaccination, including for broad protection against SARS-CoV-2 or other emerging coronaviruses.
Bio:
Mark Howarth has been a group leader in Oxford University Department of Biochemistry since 2007. In 2017 he spun-out the company SpyBiotech, applying peptide superglue to enhance vaccine development, and was awarded the Royal Society of Chemistry Norman Heatley prize. 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 engineering of bacterial peptide superglues. These tools are being applied to immuno-engineering, enzyme stabilization, and cell therapy.