The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase

The NDM-1 metallo-β-lactamase confers resistance to β-lactam antibiotics. Here, the authors show that the antimicrobial peptide thanatin is active against NDM-1-producing bacteria through a dual mechanism of action consisting of disruption of outer membrane integrity and inhibition of the NDM-1 enzy...

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Autores principales:	Bo Ma, Chao Fang, Linshan Lu, Mingzhi Wang, Xiaoyan Xue, Ying Zhou, Mingkai Li, Yue Hu, Xiaoxing Luo, Zheng Hou
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5264630a22df4ed9ae5b7ee92c052341
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spelling	oai:doaj.org-article:5264630a22df4ed9ae5b7ee92c0523412021-12-02T15:35:59ZThe antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase10.1038/s41467-019-11503-32041-1723https://doaj.org/article/5264630a22df4ed9ae5b7ee92c0523412019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11503-3https://doaj.org/toc/2041-1723The NDM-1 metallo-β-lactamase confers resistance to β-lactam antibiotics. Here, the authors show that the antimicrobial peptide thanatin is active against NDM-1-producing bacteria through a dual mechanism of action consisting of disruption of outer membrane integrity and inhibition of the NDM-1 enzymatic activity.Bo MaChao FangLinshan LuMingzhi WangXiaoyan XueYing ZhouMingkai LiYue HuXiaoxing LuoZheng HouNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Bo Ma Chao Fang Linshan Lu Mingzhi Wang Xiaoyan Xue Ying Zhou Mingkai Li Yue Hu Xiaoxing Luo Zheng Hou The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
description	The NDM-1 metallo-β-lactamase confers resistance to β-lactam antibiotics. Here, the authors show that the antimicrobial peptide thanatin is active against NDM-1-producing bacteria through a dual mechanism of action consisting of disruption of outer membrane integrity and inhibition of the NDM-1 enzymatic activity.
format	article
author	Bo Ma Chao Fang Linshan Lu Mingzhi Wang Xiaoyan Xue Ying Zhou Mingkai Li Yue Hu Xiaoxing Luo Zheng Hou
author_facet	Bo Ma Chao Fang Linshan Lu Mingzhi Wang Xiaoyan Xue Ying Zhou Mingkai Li Yue Hu Xiaoxing Luo Zheng Hou
author_sort	Bo Ma
title	The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
title_short	The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
title_full	The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
title_fullStr	The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
title_full_unstemmed	The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
title_sort	antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the ndm-1 metallo-β-lactamase
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/5264630a22df4ed9ae5b7ee92c052341
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The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase

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