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Proteolysis of recombinant proteins in bioengineered plant cells

Plants are increasingly used as alternative expression hosts for the production of recombinant proteins offering many advantages including higher biomass and the ability to perform post-translational modifications on complex proteins. Key challenges for optimized accumulation of recombinant proteins...

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Detalles Bibliográficos
Autores principales: Pillay, Priyen, Schlüter, Urte, van Wyk, Stefan, Kunert, Karl Josef, Vorster, Barend Juan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4008460/
https://www.ncbi.nlm.nih.gov/pubmed/23778319
http://dx.doi.org/10.4161/bioe.25158
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author Pillay, Priyen
Schlüter, Urte
van Wyk, Stefan
Kunert, Karl Josef
Vorster, Barend Juan
author_facet Pillay, Priyen
Schlüter, Urte
van Wyk, Stefan
Kunert, Karl Josef
Vorster, Barend Juan
author_sort Pillay, Priyen
collection PubMed
description Plants are increasingly used as alternative expression hosts for the production of recombinant proteins offering many advantages including higher biomass and the ability to perform post-translational modifications on complex proteins. Key challenges for optimized accumulation of recombinant proteins in a plant system still remain, including endogenous plant proteolytic activity, which may severely compromise recombinant protein stability. Several strategies have recently been applied to improve protein stability by limiting protease action such as recombinant protein production in various sub-cellular compartments or application of protease inhibitors to limit protease action. A short update on the current strategies applied is provided here, with particular focus on sub-cellular sites previously selected for recombinant protein production and the co-expression of protease inhibitors to limit protease activity.
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spelling pubmed-40084602014-05-05 Proteolysis of recombinant proteins in bioengineered plant cells Pillay, Priyen Schlüter, Urte van Wyk, Stefan Kunert, Karl Josef Vorster, Barend Juan Bioengineered Review Plants are increasingly used as alternative expression hosts for the production of recombinant proteins offering many advantages including higher biomass and the ability to perform post-translational modifications on complex proteins. Key challenges for optimized accumulation of recombinant proteins in a plant system still remain, including endogenous plant proteolytic activity, which may severely compromise recombinant protein stability. Several strategies have recently been applied to improve protein stability by limiting protease action such as recombinant protein production in various sub-cellular compartments or application of protease inhibitors to limit protease action. A short update on the current strategies applied is provided here, with particular focus on sub-cellular sites previously selected for recombinant protein production and the co-expression of protease inhibitors to limit protease activity. Landes Bioscience 2014-01-01 2013-05-29 /pmc/articles/PMC4008460/ /pubmed/23778319 http://dx.doi.org/10.4161/bioe.25158 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Review
Pillay, Priyen
Schlüter, Urte
van Wyk, Stefan
Kunert, Karl Josef
Vorster, Barend Juan
Proteolysis of recombinant proteins in bioengineered plant cells
title Proteolysis of recombinant proteins in bioengineered plant cells
title_full Proteolysis of recombinant proteins in bioengineered plant cells
title_fullStr Proteolysis of recombinant proteins in bioengineered plant cells
title_full_unstemmed Proteolysis of recombinant proteins in bioengineered plant cells
title_short Proteolysis of recombinant proteins in bioengineered plant cells
title_sort proteolysis of recombinant proteins in bioengineered plant cells
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4008460/
https://www.ncbi.nlm.nih.gov/pubmed/23778319
http://dx.doi.org/10.4161/bioe.25158
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