ArticleNature communications2019
Spy&Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
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- Catcher Domains as Multifunctional Fusion Modules for Soluble Expression, Covalent Coupling, and Spatial Organization of Recombinant Proteins.Small science · 2026Article
- Development of SpyTag/SpyCatcher-driven thermostable cyclic laccase and its application in lignin and dye degradation and polymerization of phenolic compounds.Science China. Life sciences · 2026Article
- Characterization of gRNA-dependent and gRNA-independent off-target binding sites of PspCas13b and RfxCas13d in mammalian cells.Nucleic acids research · 2026Article
- Membrane curvature initiates Cdc42-FBP17-N-WASP clustering and actin nucleation.The EMBO journal · 2026Article
- Induced Proximity Approach Enables the Recombinant Production of Polyphosphorylated Silk Proteins with Improved Adhesiveness.Biomacromolecules · 2025Article
- Protein nanocages: A new frontier in mucosal vaccine delivery and immune activation.Human vaccines & immunotherapeutics · 2025Review
- A bivalent Mpox nanoparticle vaccine induces robust immune response and provides long-lasting protection against vaccinia virus challenge.Emerging microbes & infections · 2025Article
- Multifunctional Nanobody Fusion Proteins in Immunoassays: Diverse Strategies for Enhanced Analytical Performance.Trends in analytical chemistry : TRAC · 2025Article
- DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminus.Molecular biology of the cell · 2025Article
- Click biology highlights the opportunities from reliable biological reactions.Nature chemical biology · 2025Review
- A Novel Chitin-Based Purification System Using GAL1 Fusion Tags: Enhancing Recombinant Protein Production While Retaining Biological Activity.Microbial biotechnology · 2025Article
- A Robust and Easy Protein Purification Method Using SpyDock-Modified Resin.Bio-protocol · 2025Article
- Advances and Challenges in the Development of Immobilized Enzymes for Batch and Flow Biocatalyzed Processes.ChemSusChem · 2025Review
- A Comprehensive Guide to Enzyme Immobilization: All You Need to Know.Molecules (Basel, Switzerland) · 2025Review
- Advances in nanobody multimerization and multispecificity: from in vivo assembly to in vitro production.Biochemical Society transactions · 2025Review
- DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminal tail.bioRxiv : the preprint server for biology · 2024Article
- RNA scaffolds the Golgi ribbon by forming condensates with GM130.Nature cell biology · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide tags are a key resource, introducing minimal change while enabling a consistent process to purify diverse proteins. However, peptide tags often provide minimal benefit post-purification. We previously designed SpyTag, forming an irreversible bond with its protein partner SpyCatcher. SpyTag provides an easy route to anchor, bridge or multimerize proteins. Here we establish Spy&Go, enabling protein purification using SpyTag. Through rational engineering we generated SpyDock, which captures SpyTag-fusions and allows efficient elution. Spy&Go enabled sensitive purification of SpyTag-fusions from Escherichia coli, giving superior purity than His-tag/nickel-nitrilotriacetic acid. Spy&Go allowed purification of mammalian-expressed, N-terminal, C-terminal or internal SpyTag. As an oligomerization toolbox, we established a panel of SpyCatcher-linked coiled coils, so SpyTag-fusions can be dimerized, trimerized, tetramerized, pentamerized, hexamerized or heptamerized. Assembling oligomers for Death Receptor 5 stimulation, we probed multivalency effects on cancer cell death. Spy&Go, combined with simple oligomerization, should have broad application for exploring multivalency in signaling.
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