Insider information on successful covalent protein coupling with help from SpyBank

Methods Enzymol. 2019:617:443-461. doi: 10.1016/bs.mie.2018.12.010. Epub 2019 Jan 25.

Abstract

New biological properties can stem from the freedom to link, multimerize, or multiplex protein building blocks. The peptide SpyTag on one protein irreversibly reacts with SpyCatcher on another protein, through spontaneous isopeptide bond formation. Reaction is specific in a wide range of cellular environments and all components are genetically encoded, making this chemistry accessible to molecular biologists. SpyTag/SpyCatcher has been widely used for enzyme immobilization, colocalization of different enzymatic activities, and increasing enzyme resilience. Here we present routes and advice for efficient design, expression, and purification of SpyTag/SpyCatcher constructs in bacterial and eukaryotic environments, including the latest 002 variants, and how to analyze reaction efficiency. The SpyInfo webpage collates the different publications and patents using SpyTag/SpyCatcher, while the SpyBank database lists their sequences and expression routes. The ability of SpyTag/SpyCatcher to react in a broad range of situations creates diverse opportunities for augmenting the function of enzymes and other biomolecules.

Keywords: Metabolite channeling; Nanoassembly; Nanobiotechnology; Plug-and-display; Protein engineering; Protein superglue; Protein–protein interaction; Synthetic biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western / methods
  • Databases, Protein
  • Electrophoresis, Polyacrylamide Gel / methods
  • Escherichia coli / genetics
  • Gene Expression
  • HEK293 Cells
  • Humans
  • Peptides / chemistry
  • Peptides / genetics*
  • Protein Engineering / methods
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics

Substances

  • Peptides
  • Recombinant Fusion Proteins
  • SpyTag peptide