Direct N- or C-Terminal Protein Labeling Via a Sortase-Mediated Swapping Approach

Bioconjug Chem. 2021 Nov 17;32(11):2397-2406. doi: 10.1021/acs.bioconjchem.1c00442. Epub 2021 Nov 8.

Abstract

Site-specific protein labeling is important in biomedical research and biotechnology. While many methods allow site-specific protein modification, a straightforward approach for efficient N-terminal protein labeling is not available. We introduce a novel sortase-mediated swapping approach for a one-step site-specific N-terminal labeling with a near-quantitative yield. We show that this method allows rapid and efficient cleavage and simultaneous labeling of the N or C termini of fusion proteins. The method does not require any prior modification beyond the genetic incorporation of the sortase recognition motif. This new approach provides flexibility for protein engineering and site-specific protein modifications.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aminoacyltransferases* / chemistry
  • Aminoacyltransferases* / genetics
  • Aminoacyltransferases* / metabolism
  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Cysteine Endopeptidases* / chemistry
  • Cysteine Endopeptidases* / genetics
  • Cysteine Endopeptidases* / metabolism
  • Protein Engineering / methods
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Staining and Labeling / methods

Substances

  • Aminoacyltransferases
  • Cysteine Endopeptidases
  • Bacterial Proteins
  • sortase A
  • Recombinant Fusion Proteins