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Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming

Although the field of molecular farming has significantly matured over the last years, some obstacles still need to be resolved. A major limiting factor for a broader application of plant hosts for the production of valuable recombinant proteins is the low yield of intact recombinant proteins. These...

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Autores principales: Mandal, Manoj K., Ahvari, Houtan, Schillberg, Stefan, Schiermeyer, Andreas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4782010/
https://www.ncbi.nlm.nih.gov/pubmed/27014293
http://dx.doi.org/10.3389/fpls.2016.00267
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author Mandal, Manoj K.
Ahvari, Houtan
Schillberg, Stefan
Schiermeyer, Andreas
author_facet Mandal, Manoj K.
Ahvari, Houtan
Schillberg, Stefan
Schiermeyer, Andreas
author_sort Mandal, Manoj K.
collection PubMed
description Although the field of molecular farming has significantly matured over the last years, some obstacles still need to be resolved. A major limiting factor for a broader application of plant hosts for the production of valuable recombinant proteins is the low yield of intact recombinant proteins. These low yields are at least in part due to the action of endogenous plant proteases on the foreign recombinant proteins. This mini review will present the current knowledge of the proteolytic enzymes involved in the degradation of different target proteins and strategies that are applied to suppress undesirable proteolytic activities in order to safeguard recombinant proteins during the production process.
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spelling pubmed-47820102016-03-24 Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming Mandal, Manoj K. Ahvari, Houtan Schillberg, Stefan Schiermeyer, Andreas Front Plant Sci Plant Science Although the field of molecular farming has significantly matured over the last years, some obstacles still need to be resolved. A major limiting factor for a broader application of plant hosts for the production of valuable recombinant proteins is the low yield of intact recombinant proteins. These low yields are at least in part due to the action of endogenous plant proteases on the foreign recombinant proteins. This mini review will present the current knowledge of the proteolytic enzymes involved in the degradation of different target proteins and strategies that are applied to suppress undesirable proteolytic activities in order to safeguard recombinant proteins during the production process. Frontiers Media S.A. 2016-03-08 /pmc/articles/PMC4782010/ /pubmed/27014293 http://dx.doi.org/10.3389/fpls.2016.00267 Text en Copyright © 2016 Mandal, Ahvari, Schillberg and Schiermeyer. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Mandal, Manoj K.
Ahvari, Houtan
Schillberg, Stefan
Schiermeyer, Andreas
Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming
title Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming
title_full Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming
title_fullStr Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming
title_full_unstemmed Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming
title_short Tackling Unwanted Proteolysis in Plant Production Hosts Used for Molecular Farming
title_sort tackling unwanted proteolysis in plant production hosts used for molecular farming
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4782010/
https://www.ncbi.nlm.nih.gov/pubmed/27014293
http://dx.doi.org/10.3389/fpls.2016.00267
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