A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli

Abstract Antimicrobial peptides, promising antibiotic candidates, are attracting increasing research attention. Current methods for production of antimicrobial peptides are chemical synthesis, intracellular fusion expression, or direct separation and purification from natural sources. However, all t...

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Autores principales:	Meng Wang, Minhua Huang, Junjie Zhang, Yi Ma, Shan Li, Jufang Wang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e50349fde05e41d2bc228e0005ded573
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spelling	oai:doaj.org-article:e50349fde05e41d2bc228e0005ded5732021-12-02T11:52:37ZA novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli10.1038/s41598-017-07411-52045-2322https://doaj.org/article/e50349fde05e41d2bc228e0005ded5732017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07411-5https://doaj.org/toc/2045-2322Abstract Antimicrobial peptides, promising antibiotic candidates, are attracting increasing research attention. Current methods for production of antimicrobial peptides are chemical synthesis, intracellular fusion expression, or direct separation and purification from natural sources. However, all these methods are costly, operation-complicated and low efficiency. Here, we report a new strategy for extracellular secretion and online-cleavage of antimicrobial peptides on the surface of Escherichia coli, which is cost-effective, simple and does not require complex procedures like cell disruption and protein purification. Analysis by transmission electron microscopy and semi-denaturing detergent agarose gel electrophoresis indicated that fusion proteins contain cecropin A peptides can successfully be secreted and form extracellular amyloid aggregates at the surface of Escherichia coli on the basis of E. coli curli secretion system and amyloid characteristics of sup35NM. These amyloid aggregates can be easily collected by simple centrifugation and high-purity cecropin A peptide with the same antimicrobial activity as commercial peptide by chemical synthesis was released by efficient self-cleavage of Mxe GyrA intein. Here, we established a novel expression strategy for the production of antimicrobial peptides, which dramatically reduces the cost and simplifies purification procedures and gives new insights into producing antimicrobial and other commercially-viable peptides.Meng WangMinhua HuangJunjie ZhangYi MaShan LiJufang WangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Meng Wang Minhua Huang Junjie Zhang Yi Ma Shan Li Jufang Wang A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli
description	Abstract Antimicrobial peptides, promising antibiotic candidates, are attracting increasing research attention. Current methods for production of antimicrobial peptides are chemical synthesis, intracellular fusion expression, or direct separation and purification from natural sources. However, all these methods are costly, operation-complicated and low efficiency. Here, we report a new strategy for extracellular secretion and online-cleavage of antimicrobial peptides on the surface of Escherichia coli, which is cost-effective, simple and does not require complex procedures like cell disruption and protein purification. Analysis by transmission electron microscopy and semi-denaturing detergent agarose gel electrophoresis indicated that fusion proteins contain cecropin A peptides can successfully be secreted and form extracellular amyloid aggregates at the surface of Escherichia coli on the basis of E. coli curli secretion system and amyloid characteristics of sup35NM. These amyloid aggregates can be easily collected by simple centrifugation and high-purity cecropin A peptide with the same antimicrobial activity as commercial peptide by chemical synthesis was released by efficient self-cleavage of Mxe GyrA intein. Here, we established a novel expression strategy for the production of antimicrobial peptides, which dramatically reduces the cost and simplifies purification procedures and gives new insights into producing antimicrobial and other commercially-viable peptides.
format	article
author	Meng Wang Minhua Huang Junjie Zhang Yi Ma Shan Li Jufang Wang
author_facet	Meng Wang Minhua Huang Junjie Zhang Yi Ma Shan Li Jufang Wang
author_sort	Meng Wang
title	A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli
title_short	A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli
title_full	A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli
title_fullStr	A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli
title_full_unstemmed	A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli
title_sort	novel secretion and online-cleavage strategy for production of cecropin a in escherichia coli
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/e50349fde05e41d2bc228e0005ded573
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A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli

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