ArticleProceedings of the National Academy of Sciences of the United States of America2014
Reprogramming the specificity of sortase enzymes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed.
- A Genetically Encoded Electrophilic Lysine Derivative Enables Sortase-Mediated Assembly of SUMO Activity-Based Probes.Journal of the American Chemical Society · 2026Article
- Rank-guided learning accelerates automated enzyme engineering.Nature communications · 2026Article
- Boolean Logic-Based Control Over Recombinant Protein Biomaterial Degradability and Therapeutic Delivery.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Substrate biasing in UCHL5 proteoforms.bioRxiv : the preprint server for biology · 2026Article
- One-Pot Orthogonal Dual Functionalization of mi3 Self-Assembling Protein Nanoparticles via Sortase A and SpyCatcher/SpyTag Ligation.Bioconjugate chemistry · 2026Article
- Self-assembling protein nanoparticles for cytosolic delivery of nucleic acids and proteins.Nature biotechnology · 2026Article
- Sortase A Catalyzed Transpeptidation for Protein Bioengineering.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Library-on-Library Intercellular Labeling for Selection of Biotin Ligase and Acceptor Peptides.Chembiochem : a European journal of chemical biology · 2026Article
- Homogeneous antibody-drug conjugates with dual payloads: potential, methods and considerations.mAbs · 2025Review
- Enzymatic Methods for Assembling and Modifying Hydrogel Biomaterials.Regenerative engineering and translational medicine · 2025Article
- Boolean logic-gated protein presentation through autonomously compiled molecular topology.Nature chemical biology · 2025Article
- Protease engineering: Approaches, tools, and emerging trends.Biotechnology advances · 2025Review
- Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini.Nature chemistry · 2025Article
- Site-directed multivalent conjugation of antibodies to ubiquitinated payloads.Nature biomedical engineering · 2025Article
- Data-driven protease engineering by DNA-recording and epistasis-aware machine learning.Nature communications · 2025Article
- Matrix Stiffness and Biochemistry Govern Colorectal Cancer Cell Growth and Signaling in User-Programmable Synthetic Hydrogels.ACS biomaterials science & engineering · 2025Article
- Proximity Labeling of Cell Surface Proteins via Cell Surface Remodeling.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Application of Sortase-Mediated Ligation for the Synthesis of Block Copolymers and Protein-Polymer Conjugates.Macromolecular bioscience · 2025Article
- Site-Specific and Fluorescently Enhanced Installation of Post-Translational Protein Modifications via Bifunctional Biarsenical Linker.ACS omega · 2024Article
- Protein semisynthesis reveals plasticity in HECT E3 ubiquitin ligase mechanisms.Nature chemistry · 2024Article
37 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
Staphylococcus aureus sortase A catalyzes the transpeptidation of an LPXTG peptide acceptor and a glycine-linked peptide donor and has proven to be a powerful tool for site-specific protein modification. The substrate specificity of sortase A is stringent, limiting its broader utility. Here we report the laboratory evolution of two orthogonal sortase A variants that recognize each of two altered substrates, LAXTG and LPXSG, with high activity and specificity. Following nine rounds of yeast display screening integrated with negative selection, the evolved sortases exhibit specificity changes of up to 51,000-fold, relative to the starting sortase without substantial loss of catalytic activity, and with up to 24-fold specificity for their target substrates, relative to their next most active peptide substrate. The specificities of these altered sortases are sufficiently orthogonal to enable the simultaneous conjugation of multiple peptide substrates to their respective targets in a single solution. We demonstrated the utility of these evolved sortases by using them to effect the site-specific modification of endogenous fetuin A in human plasma, the synthesis of tandem fluorophore-protein-PEG conjugates for two therapeutically relevant fibroblast growth factor proteins (FGF1 and FGF2), and the orthogonal conjugation of fluorescent peptides onto surfaces.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.