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Professor Mark Sansom, Head of Department
New tentacle method captures tumour cells with increased efficiency
The development of an improved ‘superglue’ technology by Dr Mark Howarth and his group could help in cell capture approaches aimed at detecting and treating cancer.
Dr Howarth together with DPhil students Gianluca Veggiani and Jacob Fierer have published their work in PNAS (1). They describe the new tool, developed from an earlier approach in which they engineered a stable interaction that could be used to lock molecules together.
The original method, SpyTag/SpyCatcher, was published in 2012 (2) and has already found a number of uses. It was developed from an adhesion protein found in Streptococcus pyogenes which locks itself together. The group took a domain of the protein and split it into two parts to create protein-peptide ligation between a peptide tag (SpyTag) and a protein domain (SpyCatcher).
As a covalent and irreversible interaction, the SpyTag/SpyCatcher ligation has a major advantage over other types of engineered interactions. But it also has a drawback which the new system addresses.
‘The protein domain is quite big and may interfere with protein folding and function,’ explains Gianluca Veggiani. ‘In the new scenario, we split the domain into 3 partners – two peptide tags and a protein domain. The protein domain is only required to catalyse the reaction and form the bond.’
With this bulky domain required only transiently now, the new system, called ‘SpyLigase’, allows assemblies of proteins to be built up.