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Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli

BACKGROUND: The pET expression system based on T7 promoter which is induced by isopropyl-β-D-1-thiogalactopyranoside (IPTG) is by far the most commonly used system for production of heterogeneous proteins in Escherichia coli. However, this system was limited by obvious drawbacks including the host t...

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Autores principales: Shang, Fei, Wang, Hui, Zhang, Dan, Wang, Wenhui, Yu, Jiangliu, Xue, Ting
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8603832/
https://www.ncbi.nlm.nih.gov/pubmed/34820206
http://dx.doi.org/10.7717/peerj.12497
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author Shang, Fei
Wang, Hui
Zhang, Dan
Wang, Wenhui
Yu, Jiangliu
Xue, Ting
author_facet Shang, Fei
Wang, Hui
Zhang, Dan
Wang, Wenhui
Yu, Jiangliu
Xue, Ting
author_sort Shang, Fei
collection PubMed
description BACKGROUND: The pET expression system based on T7 promoter which is induced by isopropyl-β-D-1-thiogalactopyranoside (IPTG) is by far the most commonly used system for production of heterogeneous proteins in Escherichia coli. However, this system was limited by obvious drawbacks including the host toxicity and metabolic burden imposed by the presence of IPTG. METHODS: In this study, we incorporated the autoinducer-2 (AI-2) quorum sensing system to realize autoinduction of the pET expression system. The autoinduction expression vector pXWZ1 was constructed by inserting the lsr promoter regions into the pET28a(+) vector. The expression efficiency of the reporter genes gfpuv and lacZ by the pXWZ1 and pET28a(+) vectors were compared. RESULTS: The results showed that the expression levels of the both report genes in the cells transformed with pXWZ1 without any addition of exogenous inducer were higher than that transformed with pET28a(+) vectors by the induction of IPTG. CONCLUSION: This new auto-induction system will exclude the limitations of the IPTG induction including toxic to host and increasing formation of inclusion body and will become a more economical and convenient tool for recombinant protein expression.
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spelling pubmed-86038322021-11-23 Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli Shang, Fei Wang, Hui Zhang, Dan Wang, Wenhui Yu, Jiangliu Xue, Ting PeerJ Biotechnology BACKGROUND: The pET expression system based on T7 promoter which is induced by isopropyl-β-D-1-thiogalactopyranoside (IPTG) is by far the most commonly used system for production of heterogeneous proteins in Escherichia coli. However, this system was limited by obvious drawbacks including the host toxicity and metabolic burden imposed by the presence of IPTG. METHODS: In this study, we incorporated the autoinducer-2 (AI-2) quorum sensing system to realize autoinduction of the pET expression system. The autoinduction expression vector pXWZ1 was constructed by inserting the lsr promoter regions into the pET28a(+) vector. The expression efficiency of the reporter genes gfpuv and lacZ by the pXWZ1 and pET28a(+) vectors were compared. RESULTS: The results showed that the expression levels of the both report genes in the cells transformed with pXWZ1 without any addition of exogenous inducer were higher than that transformed with pET28a(+) vectors by the induction of IPTG. CONCLUSION: This new auto-induction system will exclude the limitations of the IPTG induction including toxic to host and increasing formation of inclusion body and will become a more economical and convenient tool for recombinant protein expression. PeerJ Inc. 2021-11-16 /pmc/articles/PMC8603832/ /pubmed/34820206 http://dx.doi.org/10.7717/peerj.12497 Text en ©2021 Shang et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biotechnology
Shang, Fei
Wang, Hui
Zhang, Dan
Wang, Wenhui
Yu, Jiangliu
Xue, Ting
Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli
title Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli
title_full Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli
title_fullStr Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli
title_full_unstemmed Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli
title_short Construction of an AI-2 quorum sensing induced heterologous protein expression system in Escherichia coli
title_sort construction of an ai-2 quorum sensing induced heterologous protein expression system in escherichia coli
topic Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8603832/
https://www.ncbi.nlm.nih.gov/pubmed/34820206
http://dx.doi.org/10.7717/peerj.12497
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