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A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System

Cell surface display systems for immobilization of peptides and proteins on the surface of cells have various applications, such as vaccine generation, protein engineering, bio-conversion and bio-adsorption. Though plenty of methods have been established in terms of traditional yeast surface display...

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Detalles Bibliográficos
Autores principales: Li, Shuntang, Qiao, Jie, Lin, Siyu, Liu, Yi, Ma, Lixin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6514646/
https://www.ncbi.nlm.nih.gov/pubmed/30991754
http://dx.doi.org/10.3390/molecules24081483
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author Li, Shuntang
Qiao, Jie
Lin, Siyu
Liu, Yi
Ma, Lixin
author_facet Li, Shuntang
Qiao, Jie
Lin, Siyu
Liu, Yi
Ma, Lixin
author_sort Li, Shuntang
collection PubMed
description Cell surface display systems for immobilization of peptides and proteins on the surface of cells have various applications, such as vaccine generation, protein engineering, bio-conversion and bio-adsorption. Though plenty of methods have been established in terms of traditional yeast surface display systems, the development of a universal display method with high efficiency remains a challenge. Here we report an indirect yeast surface display method by anchoring Im7 proteins on the surface of P. pastoris, achieving highly efficient display of target proteins, including fluorescence proteins (sfGFP and mCherry) or enzymes (human Arginase I), with a CL7 fusion tag through the ultra-high-affinity interaction between Im7 and CL7. This indirect P. pastoris surface display approach is highly efficient and provides a robust platform for displaying biomolecules.
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spelling pubmed-65146462019-05-30 A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System Li, Shuntang Qiao, Jie Lin, Siyu Liu, Yi Ma, Lixin Molecules Article Cell surface display systems for immobilization of peptides and proteins on the surface of cells have various applications, such as vaccine generation, protein engineering, bio-conversion and bio-adsorption. Though plenty of methods have been established in terms of traditional yeast surface display systems, the development of a universal display method with high efficiency remains a challenge. Here we report an indirect yeast surface display method by anchoring Im7 proteins on the surface of P. pastoris, achieving highly efficient display of target proteins, including fluorescence proteins (sfGFP and mCherry) or enzymes (human Arginase I), with a CL7 fusion tag through the ultra-high-affinity interaction between Im7 and CL7. This indirect P. pastoris surface display approach is highly efficient and provides a robust platform for displaying biomolecules. MDPI 2019-04-15 /pmc/articles/PMC6514646/ /pubmed/30991754 http://dx.doi.org/10.3390/molecules24081483 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Li, Shuntang
Qiao, Jie
Lin, Siyu
Liu, Yi
Ma, Lixin
A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System
title A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System
title_full A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System
title_fullStr A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System
title_full_unstemmed A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System
title_short A Highly Efficient Indirect P. pastoris Surface Display Method Based on the CL7/Im7 Ultra-High-Affinity System
title_sort highly efficient indirect p. pastoris surface display method based on the cl7/im7 ultra-high-affinity system
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6514646/
https://www.ncbi.nlm.nih.gov/pubmed/30991754
http://dx.doi.org/10.3390/molecules24081483
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