Modification of bacterial microcompartments with target biomolecules via post-translational SpyTagging

David M. Beal, Mingzhi Liang, Ian Brown, James D. Budge, Emily R. Burrows, Kevin Howland, Phoebe Lee, Sarah Martin, Andrew Morrell, Emi Nemoto-Smith, Joanne Roobol, Maria Stanley, C. Mark Smales, Martin J. Warren

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Bacterial microcompartments (BMCs) are proteinaceous organelle-like structures formed within bacteria, often encapsulating enzymes and cellular processes, in particular, allowing toxic intermediates to be shielded from the general cellular environment. Outside of their biological role they are of interest, through surface modification, as potential drug carriers and polyvalent antigen display scaffolds. Here we use a post-translational modification approach, using copper free click chemistry, to attach a SpyTag to a target protein molecule for attachment to a specific SpyCatcher modified BMC shell protein. We demonstrate that a post-translationally SpyTagged material can react with a SpyCatcher modified BMC and show its presence on the surface of BMCs, enabling future investigation of these structures as polyvalent antigen display scaffolds for vaccine development. This post-translational ‘click’ methodology overcomes the necessity to genetically encode the SpyTag, avoids any potential reduction in expression yield and expands the scope of SpyTag/SpyCatcher vaccine scaffolds to form peptide epitope vaccines and small molecule delivery agents.
Original languageEnglish
Pages (from-to)2963-2970
Number of pages8
JournalMaterials Advances
Volume4
Issue number14
Early online date12 Jun 2023
DOIs
Publication statusPublished - 17 Jul 2023

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