Protein-Protein Fusion Catalyzed by Sortase A
Open Access
- 6 April 2011
- journal article
- research article
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 6 (4), e18342
- https://doi.org/10.1371/journal.pone.0018342
Abstract
Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligation and report the successful fusion of 10 pairs of protein domains with preserved functionality — demonstrating the robust and facile nature of this reaction.Keywords
This publication has 31 references indexed in Scilit:
- Sortase-catalyzed transformations that improve the properties of cytokinesProceedings of the National Academy of Sciences, 2011
- Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopyJournal of Biomolecular NMR, 2010
- Stability and CDR Composition Biases Enrich Binder Functionality LandscapesJournal of Molecular Biology, 2010
- A modular IgG-scFv bispecific antibody topologyProtein Engineering, Design and Selection, 2009
- Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisationBiotechnology Letters, 2009
- Site‐Specific Protein Labeling via Sortase‐Mediated TranspeptidationCurrent Protocols in Protein Science, 2009
- Lipid Modification of Proteins through Sortase-Catalyzed TranspeptidationJournal of the American Chemical Society, 2008
- Mutagenesis Studies of Substrate Recognition and Catalysis in the Sortase A Transpeptidase from Staphylococcus aureusJournal of Biological Chemistry, 2008
- Covalent Attachment of Proteins to Solid Supports and Surfaces via Sortase-Mediated LigationPLOS ONE, 2007
- Synthesis of Biologically Active Peptide Nucleic Acid−Peptide Conjugates by Sortase-Mediated LigationThe Journal of Organic Chemistry, 2007