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Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability

The production of therapeutic and industrial recombinant proteins in plants has advantages over established bacterial and mammalian systems in terms of cost, scalability, growth conditions, and product safety. In order to compete with these conventional expression systems, however, plant expression...

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Detalles Bibliográficos
Autores principales: Feng, Ziru, Li, Xifeng, Fan, Baofang, Zhu, Cheng, Chen, Zhixiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9659199/
https://www.ncbi.nlm.nih.gov/pubmed/36362299
http://dx.doi.org/10.3390/ijms232113516
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author Feng, Ziru
Li, Xifeng
Fan, Baofang
Zhu, Cheng
Chen, Zhixiang
author_facet Feng, Ziru
Li, Xifeng
Fan, Baofang
Zhu, Cheng
Chen, Zhixiang
author_sort Feng, Ziru
collection PubMed
description The production of therapeutic and industrial recombinant proteins in plants has advantages over established bacterial and mammalian systems in terms of cost, scalability, growth conditions, and product safety. In order to compete with these conventional expression systems, however, plant expression platforms must have additional economic advantages by demonstrating a high protein production yield with consistent quality. Over the past decades, important progress has been made in developing strategies to increase the yield of recombinant proteins in plants by enhancing their expression and reducing their degradation. Unlike bacterial and animal systems, plant expression systems can utilize not only cell cultures but also whole plants for the production of recombinant proteins. The development of viral vectors and chloroplast transformation has opened new strategies to drastically increase the yield of recombinant proteins from plants. The identification of promoters for strong, constitutive, and inducible promoters or the tissue-specific expression of transgenes allows for the production of recombinant proteins at high levels and for special purposes. Advances in the understanding of RNAi have led to effective strategies for reducing gene silencing and increasing recombinant protein production. An increased understanding of protein translation, quality control, trafficking, and degradation has also helped with the development of approaches to enhance the synthesis and stability of recombinant proteins in plants. In this review, we discuss the progress in understanding the processes that control the synthesis and degradation of gene transcripts and proteins, which underlie a variety of developed strategies aimed at maximizing recombinant protein production in plants.
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spelling pubmed-96591992022-11-15 Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability Feng, Ziru Li, Xifeng Fan, Baofang Zhu, Cheng Chen, Zhixiang Int J Mol Sci Review The production of therapeutic and industrial recombinant proteins in plants has advantages over established bacterial and mammalian systems in terms of cost, scalability, growth conditions, and product safety. In order to compete with these conventional expression systems, however, plant expression platforms must have additional economic advantages by demonstrating a high protein production yield with consistent quality. Over the past decades, important progress has been made in developing strategies to increase the yield of recombinant proteins in plants by enhancing their expression and reducing their degradation. Unlike bacterial and animal systems, plant expression systems can utilize not only cell cultures but also whole plants for the production of recombinant proteins. The development of viral vectors and chloroplast transformation has opened new strategies to drastically increase the yield of recombinant proteins from plants. The identification of promoters for strong, constitutive, and inducible promoters or the tissue-specific expression of transgenes allows for the production of recombinant proteins at high levels and for special purposes. Advances in the understanding of RNAi have led to effective strategies for reducing gene silencing and increasing recombinant protein production. An increased understanding of protein translation, quality control, trafficking, and degradation has also helped with the development of approaches to enhance the synthesis and stability of recombinant proteins in plants. In this review, we discuss the progress in understanding the processes that control the synthesis and degradation of gene transcripts and proteins, which underlie a variety of developed strategies aimed at maximizing recombinant protein production in plants. MDPI 2022-11-04 /pmc/articles/PMC9659199/ /pubmed/36362299 http://dx.doi.org/10.3390/ijms232113516 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Feng, Ziru
Li, Xifeng
Fan, Baofang
Zhu, Cheng
Chen, Zhixiang
Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability
title Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability
title_full Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability
title_fullStr Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability
title_full_unstemmed Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability
title_short Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability
title_sort maximizing the production of recombinant proteins in plants: from transcription to protein stability
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9659199/
https://www.ncbi.nlm.nih.gov/pubmed/36362299
http://dx.doi.org/10.3390/ijms232113516
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