A tethered yeast surface display system facilitates enriching epitope-specific binding interactions.

Rojhae A Panton, Jakob Lind, Amanda Richardson, Isabela Panozzo, Daniela Gomez Garcia, Syed Muzaffar, Lawrence A Stern

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Article in Protein engineering, design & selection : PEDS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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7 authors.

Rojhae A PantonDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.

Jakob LindDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.

Amanda RichardsonDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.

Isabela PanozzoDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.

Daniela Gomez GarciaDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.

Syed MuzaffarDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.

Lawrence A SternDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33620, United States.ORCID 0000-0002-3369-7495

Funding

High-Throughput Platforms to Study Synthetic Receptors, Natural Molecules, and New Pathway InhibitorsR35GM147104 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI Lawrence A Stern · 2022 to 2026

$1.8M

NIGMS NIH HHS R35 GM147104NIH National Institute of General Medical Sciences Maximizing Investigators' Research Award R35GM147104University of South FloridaUniversity of South Florida New Researcher

6 · The paper itself

Abstract

Engineering proteins for therapeutic applications is a field that has seen substantial growth in the past two decades, but challenges remain. A major deficiency in current strategies is the lack of a means to efficiently screen for binding to key epitopes to yield a desired function. To meet this challenge, we designed a tethered yeast surface display construct that leverages high local concentrations by tethering a candidate protein binder to a target protein of interest (POI) via a flexible peptide linker. These high local concentrations enable screening of epitope-specific binders based on decreased signal due to inhibitory function when the construct is assayed alongside a competitive POI binder. We demonstrate that epitope-specific screening and enrichment is possible based on fluorescent output and study key optimization parameters. We anticipate this technique will accelerate binder development by reducing the need for downstream low throughput epitope mapping of isolated proteins.

Indexed as

Cell Surface Display TechniquesEpitopesProtein EngineeringSaccharomyces cerevisiaeEpitope MappingProtein BindingEpitopesepitope specificityoptimizationtetheringyeast surface display

Identifiers

PMID42466606

DOI10.1093/protein/gzag019

PMCPMC13480473

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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.