Post-Assembly Modification of Protein Cages by Ubc9-Mediated Lysine Acylation
- Journal Article
Although viruses have been successfully repurposed as vaccines, antibiotics, and anticancer therapeutics, they also raise concerns regarding genome integration and immunogenicity. Virus-like particles and non-viral protein cages represent a potentially safer alternative but often lack desired functionality. Here, we investigated the utility of a new enzymatic bioconjugation method, called lysine acylation using conjugating enzymes (LACE), to chemoenzymatically modify protein cages. We equipped two structurally distinct protein capsules with a LACE-reactive peptide tag and demonstrated their modification with diverse ligands. This modular approach combines the advantages of chemical conjugation and genetic fusion and allows for site-specific modification with recombinant proteins as well as synthetic peptides with facile control of the extent of labeling. This strategy has the potential to fine-tune protein containers of different shape and size by providing them with new properties that go beyond their biologically native functions. Show more
Journal / seriesChemBioChem
Pages / Article No.
Subjectenzymes; LACE; lumazine synthases; protein cages; protein engineering
Organisational unit03492 - Hilvert, Donald (emeritus) / Hilvert, Donald (emeritus)
03861 - Bode, Jeffrey W. / Bode, Jeffrey W.
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