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Updated: Sep 25, 2025

Protein Engineering by Yeast Surface Display

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Engineering Proteins by Combining Deep Mutational Scanning and Yeast Display.

Preeti Sharma^1,2, Erik Procko^1,2, David M Kranz^3,4

¹Department of Biochemistry, University of Illinois, Urbana, IL, USA.

Methods in Molecular Biology (Clifton, N.J.)

|April 28, 2022

Summary

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This study combines yeast display and deep mutational scanning to engineer proteins. This powerful method reveals sequence-activity landscapes for improved therapeutic protein design.

Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Display platforms like yeast and phage display enable the discovery of proteins for therapeutic and industrial uses.
Engineering therapeutic proteins, such as antibodies and T cell receptors, often involves mutating complementarity determining regions (CDRs).
Deep mutational scanning (DMS) has emerged as a key technique for comprehensively assessing amino acid impacts across protein sequences.

Purpose of the Study:

To describe experimental methods for protein engineering by integrating yeast display with deep mutational scanning.
To provide a detailed approach for generating sequence-activity landscapes of proteins, exemplified by T cell receptors.
To highlight how this combined method can identify critical residues that might be missed by structure-based or traditional directed evolution approaches.

Keywords:

Deep mutational scanning Enrichment ratio Heat maps Protein engineering Sequence-activity landscape T cell receptors Yeast display

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Last Updated: Sep 25, 2025

Protein Engineering by Yeast Surface Display

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Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening

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Main Methods:

Utilizing yeast display to present engineered protein libraries on the cell surface.
Employing deep mutational scanning to systematically introduce and assess all possible amino acid substitutions at each position.
Combining these techniques to generate a comprehensive map of residue-specific effects on protein function, specifically for T cell receptors.

Main Results:

Demonstrated the ability to generate detailed sequence-activity landscapes for proteins.
Identified key residues (hotspots) and suboptimal sites influencing protein function, such as antigen binding in T cell receptors.
Showcased the effectiveness of integrating yeast display and DMS for uncovering engineering insights.

Conclusions:

The combination of yeast display and deep mutational scanning offers a powerful strategy for protein engineering.
This approach enables the discovery of novel protein variants with enhanced therapeutic potential.
The described methods provide a robust framework for understanding protein sequence-function relationships and optimizing protein design.