Mark Howarth, PhD, University of Oxford*

Mark Howarth, PhD
Mark Howarth, PhD

The focus of the Howarth Lab is innovating protein technologies for therapeutics and vaccine design. The lab has developed a range of ultra-stable interactions. The traptavidin system allows capture of biotinylated targets with lower off-rate and better stability to temperature or force than standard streptavidin or avidin. The SpyCatcher003 system allows rapid and spontaneous covalent bond formation to proteins bearing SpyTag or SpyTag003.

*Now affiliated with University of Cambridge.

 

Products

References

  1. Chivers CE, Crozat E, Chu C, Moy VT, Sherratt DJ, Howarth M. A streptavidin variant with slower biotin dissociation and increased mechanostability. Nature Methods 2010 May;7(5):391-93.
  2. Chivers CE, Koner AL, Lowe ED, Howarth M. How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer. 2011 Apr 1;435(1):55-63.
  3. Zakeri B, Fierer JO, Celik E, Chittock EC, Schwarz-Linek U, Moy VT, Howarth M. Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc Natl Acad Sci U S A. 2012 Mar 20;109(12):E690-7.
  4. Veggiani G., Zakeri B., Howarth M. Superglue from Bacteria: Unbreakable Bridges for Protein Nanotechnology. Trends in Biotechnology 2014 Oct;32(10):506-12.
  5. Schoene C, Fierer JO, Bennett SP, Howarth M. SpyTag/SpyCatcher Cyclization Confers Resilience to Boiling on a Mesophilic Enzyme. Angewandte Chemie. 2014 Jun 10;53(24):6101-4.
  6. Fierer JO, Veggiani G, Howarth M. SpyLigase peptide-peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture. Proc Natl Acad Sci U S A. 2014 Apr 1;111(13):E1176-81.
  7. Li L, Fierer JO, Rapoport TA, Howarth M. Structural analysis and optimization of the covalent association between SpyCatcher and a peptide tag. Journal of Molecular Biology. 2014 Jan 23;426(2):309-17.