ArticleScientific reports2019
Integrating SpyCatcher/SpyTag covalent fusion technology into phage display workflows for rapid antibody discovery.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- From bench to bedside:EJNMMI research · 2023Article
- A cell-based phenotypic library selection and screening approach for the de novo discovery of novel functional chimeric antigen receptors.Scientific reports · 2022Article
- The synergism of lytic polysaccharide monooxygenases with lichenase and their co-immobilization on silica nanospheres for green conversion of lichen biomass.Frontiers in nutrition · 2022Article
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- Soluble trivalent engagers redirect cytolytic T cell activity toward tumor endothelial marker 1.Cell reports. Medicine · 2021Article
- A novel all-in-one strategy for purification and immobilization of β-1,3-xylanase directly from cell lysate as active and recyclable nanobiocatalyst.Microbial cell factories · 2021Article
- Impact of DOTA Conjugation on Pharmacokinetics and Immunoreactivity of [Pharmaceutics · 2021Article
- Column-free purification and coating of SpyCatcher protein on ELISA wells generates universal solid support for capturing of SpyTag-fusion protein from the non-purified condition.Protein expression and purification · 2020Article
- Greatest Hits-Innovative Technologies for High Throughput Identification of Bispecific Antibodies.International journal of molecular sciences · 2020Review
- Article
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Authors and funding
6 authors.
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Abstract
An early bottleneck in the rapid isolation of new antibody fragment binders using in vitro library approaches is the inertia encountered in acquiring and preparing soluble antigen fragments. In this report, we describe a simple, yet powerful strategy that exploits the properties of the SpyCatcher/SpyTag (SpyC/SpyT) covalent interaction to improve substantially the speed and efficiency in obtaining functional antibody clones of interest. We demonstrate that SpyC has broad utility as a protein-fusion tag partner in a eukaryotic expression/secretion context, retaining its functionality and permitting the direct, selective capture and immobilization of soluble antigen fusions using solid phase media coated with a synthetic modified SpyT peptide reagent. In addition, we show that the expressed SpyC-antigen format is highly compatible with downstream antibody phage display selection and screening procedures, requiring minimal post-expression handling with no sample modifications. To illustrate the potential of the approach, we have isolated several fully human germline scFvs that selectively recognize therapeutically relevant native cell surface tumor antigens in various in vitro cell-based assay contexts.
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