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In bioengineering, scaffold proteins have been increasingly used to recruit molecules to parts of a cell, or to enhance the efficacy of biosynthetic or signalling pathways. For example, scaffolds can be used to make weak or non-immunogenic small molecules immunogenic by attaching them to the scaffold, in this role called carrier. Here, we present the dodecin from  Mycobacterium tuberculosis  ( mt Dod) as a new scaffold protein.  Mt Dod is a homododecameric complex of spherical shape, high stability and robust assembly, which allows the attachment of cargo at its surface. We show that  mt Dod, either directly loaded with cargo or equipped with domains for non-covalent and covalent loading of cargo, can be produced recombinantly in high quantity and quality in  Escherichia coli . Fusions of  mt Dod with proteins of up to four times the size of  mt Dod, e.g. with monomeric superfolder green fluorescent protein creating a 437 kDa large dodecamer, were successfully purified, showing  mt Dod’s ability to function as recruitment hub. Further,  mt Dod equipped with SYNZIP and SpyCatcher domains for post-translational recruitment of cargo was prepared of which the  mt Dod/SpyCatcher system proved to be particularly useful. In a case study, we finally show that  mt Dod-peptide fusions allow producing antibodies against human heat shock proteins and the C-terminus of heat shock cognate 70 interacting protein (CHIP).

Dodecin as carrier protein for immunizations and bioengineering applications