The SpyTag/Catcher system derives from the pathogen bacterium Streptococcus pyogenes. Thanks to the special chemical mechanism that this bacterium has developed, some of its proteins are highly stable. The surface compound SpyCatcher recognizes a small peptide chain of 13 amino acids, the SpyTag, spontaneously binding irreversibly to it through an isopeptide bond between a lysine (catcher) and an asparagine (tag) (Figure 8) [37][74][75][76]. Since both SpyTag and SpyCatcher are made of canonical amino acids, they can be linked to proteins of interest of different organisms and can also be detected by antibodies. In addition, they bind to each other extremely specifically. This covalent bond is also very stable under different pH and temperature conditions [37], which makes it a practical tool for our project. A further advantage is that the tag is short, therefore it represents a versatile system [75].
Figure 8: Formation of the SpyTag/Catcher construct. In the case of spatial proximity between SpyTag and SpyCatcher, an isopeptide bond is formed between a lysine (catcher) and an asparagine (tag), which is irreversible (structure from PDB: 4mli). Figure created with PyMOL.
The SnoopTag/Catcher system derives from a pilin of the bacterium Streptococcus pneumoniae. This system works similarly to the SpyTag/Catcher, also forming a covalent bond between a lysine and an asparagine and being constituted by short amino acid sequences. However, here the lysine can be found in the tag and the asparagine in the catcher, meaning that this toolbox is orthogonal to the SpyTag/Catcher one, since the SpyTag cannot bind to the SnoopCatcher and vice versa [75][77].
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