ArticleProtein engineering, design & selection : PEDS2021
Extended yeast surface display linkers enhance the enrichment of ligands in direct mammalian cell selections.
Article in Protein engineering, design & selection : PEDS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Identification of Variable Lymphocyte Receptors That Target the Human Blood-Brain Barrier.Pharmaceutics · 2025Article
- Engineering Affibody Binders to Death Receptor 5 and Tumor Necrosis Factor Receptor 1 With Improved Stability.Biotechnology and bioengineering · 2025Article
- Engineering Saccharomyces boulardii for enhanced surface display capacity.Microbial cell factories · 2025Article
- Binding mode-guided development of high-performance antibodies targeting site-specific posttranslational modifications.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular Display of the Animal Meta-Venome for Discovery of Novel Therapeutic Peptides.bioRxiv : the preprint server for biology · 2024Article
- Sequence-developability mapping of affibody and fibronectin paratopes via library-scale variant characterization.Protein engineering, design & selection : PEDS · 2024Article
- Flow cytometric evaluation of yeast-bacterial cell-cell interactions.Biotechnology and bioengineering · 2023Article
- Enhancing Yeast Surface Display: UPR, ERAD, and ER Dynamics in Recombinant Protein Production.Food technology and biotechnologyReview
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Authors and funding
6 authors.
Funding
Abstract
Selections of yeast-displayed ligands on mammalian cell monolayers benefit from high target expression and nanomolar affinity, which are not always available. Prior work extending the yeast-protein linker from 40 to 80 amino acids improved yield and enrichment but is hypothesized to be below the optimal length, prompting evaluation of an extended amino acid linker. A 641-residue linker provided enhanced enrichment with a 2-nM affinity fibronectin ligand and 105 epidermal growth factor receptors (EGFR) per cell (14 ± 2 vs. 8 ± 1, P = 0.008) and a >600-nM affinity ligand, 106 EGFR per cell system (23 ± 7 vs. 0.8 ± 0.2, P = 0.004). Enhanced enrichment was also observed with a 310-nM affinity affibody ligand and 104 CD276 per cell, suggesting a generalizable benefit to other scaffolds and targets. Spatial modeling of the linker suggests that improved extracellular accessibility of ligand enables the observed enrichment under conditions not previously possible.
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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.