ArticleACS synthetic biology2021
A Protein-Engineered, Enhanced Yeast Display Platform for Rapid Evolution of Challenging Targets.
Article in ACS synthetic biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 53 citations in OpenAlex.
- Stringent selection drives convergence toward omicron-like SARS-CoV-2 receptor-binding motifs.Nature communications · 2026Article
- A high-affinity split-HaloTag for live-cell protein labeling.Nature communications · 2026Article
- Modified protein selection strategy based on Escherichia coli's Hitchhiker transport and validation through selection of nanobodies targeting bovine interferon gamma.Scientific reports · 2026Article
- Engineering Saccharomyces boulardii for enhanced surface display capacity.Microbial cell factories · 2025Article
- Protein-Based Degraders: From Chemical Biology Tools to Neo-Therapeutics.Chemical reviews · 2025Review
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- Isolation of PCSK9-specific nanobodies from synthetic libraries using a combined protein selection strategy.Scientific reports · 2025Article
- The HELP-UnaG Fusion Protein as a Bilirubin Biosensor: From Theory to Mature Technological Development.Molecules (Basel, Switzerland) · 2025Review
- Optimized single-cell gates for yeast display screening.Protein engineering, design & selection : PEDS · 2025Article
- Competitive fungal commensalism mitigates candidiasis pathology.The Journal of experimental medicine · 2024Article
- Quantitative measurement of cell-surface displayed proteins based on split-GFP assembly.Microbial cell factories · 2024Article
- Protein Engineering and High-Throughput Screening by Yeast Surface Display: Survey of Current Methods.Small science · 2023Article
- Multiple mutations of SARS-CoV-2 Omicron BA.2 variant orchestrate its virological characteristics.Journal of virology · 2023Article
- Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants.Nature communications · 2023Article
- Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant.Nature communications · 2023Article
- Outer Membrane Integrity-Dependent Fluorescence of the Japanese Eel UnaG Protein in LiveBiosensors · 2023Article
- Structure and computation-guided yeast surface display for the evolution of TIMP-based matrix metalloproteinase inhibitors.Frontiers in molecular biosciences · 2023Review
- Regulation of IL-24/IL-20R2 complex formation using photocaged tyrosines and UV light.Frontiers in molecular biosciences · 2023Article
- Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant.Cell host & microbe · 2022Article
- Virological characteristics of the SARS-CoV-2 Omicron BA.2 subvariants, including BA.4 and BA.5.Cell · 2022Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we enhanced the popular yeast display method by multiple rounds of DNA and protein engineering. We introduced surface exposure-tailored reporters, eUnaG2 and DnbALFA, creating a new platform of C and N terminal fusion vectors. The optimization of eUnaG2 resulted in five times brighter fluorescence and 10 °C increased thermostability than UnaG. The optimized DnbALFA has 10-fold the level of expression of the starting protein. Following this, different plasmids were developed to create a complex platform allowing a broad range of protein expression organizations and labeling strategies. Our platform showed up to five times better separation between nonexpressing and expressing cells compared with traditional pCTcon2 and c-myc labeling, allowing for fewer rounds of selection and achieving higher binding affinities. Testing 16 different proteins, the enhanced system showed consistently stronger expression signals over c-myc labeling. In addition to gains in simplicity, speed, and cost-effectiveness, new applications were introduced to monitor protein surface exposure and protein retention in the secretion pathway that enabled successful protein engineering of hard-to-express proteins. As an example, we show how we optimized the WD40 domain of the ATG16L1 protein for yeast surface and soluble bacterial expression, starting from a nonexpressing protein. As a second example, we show how using the here-presented enhanced yeast display method we rapidly selected high-affinity binders toward two protein targets, demonstrating the simplicity of generating new protein-protein interactions. While the methodological changes are incremental, it results in a qualitative enhancement in the applicability of yeast display for many applications.
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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.