Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics

Abstract Although clinical antibiotic-resistant bacteria have attracted tremendous attention in the microbiology community, the resistant bacteria that persist in natural environments have been overlooked for a longtime. We previously proposed a new species Paramesorhizobium desertii, isolated from...

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Autores principales:	Ruichen Lv, Jingyu Guo, YanFeng Yan, Rong Chen, Lisheng Xiao, Min Wang, Nan Fang, Chengxiang Fang, Yujun Cui, Ruifu Yang, Yajun Song
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/13aac20497174f87aa96edd8e2638fa2
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spelling	oai:doaj.org-article:13aac20497174f87aa96edd8e2638fa22021-12-02T15:05:50ZCharacterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics10.1038/s41598-017-07841-12045-2322https://doaj.org/article/13aac20497174f87aa96edd8e2638fa22017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07841-1https://doaj.org/toc/2045-2322Abstract Although clinical antibiotic-resistant bacteria have attracted tremendous attention in the microbiology community, the resistant bacteria that persist in natural environments have been overlooked for a longtime. We previously proposed a new species Paramesorhizobium desertii, isolated from the soil of the Taklimakan Desert in China that is highly resistant to most β-lactam antibiotics. To identify potential β-lactamase(s) in this bacteria, we first confirmed the carbapenemase activity in the freeze–thawed supernatant of a P. desertii A-3-ET culture using the modified Hodge assay. We then identified a novel chromosome-encoded carbapenemase (PAD-1) in strain A-3-ET, using a shotgun proteomic analysis of the supernatant and genomic information. The bioinformatics analysis indicated that PAD-1 is a class A carbapenemase. Subsequent enzyme kinetic assays with purified PAD-1 confirmed its carbapenemase activity, which is similar to that of clinically significant class A carbapenemases, including BKC-1 and KPC-2. Because the location in which A-3-ET was isolated is not affected by human activity, PAD-1 is unlikely to be associated with the selection pressures exerted by modern antibiotics. This study confirmed the diversity of antibiotic-resistant determinants in the environmental resistome.Ruichen LvJingyu GuoYanFeng YanRong ChenLisheng XiaoMin WangNan FangChengxiang FangYujun CuiRuifu YangYajun SongNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ruichen Lv Jingyu Guo YanFeng Yan Rong Chen Lisheng Xiao Min Wang Nan Fang Chengxiang Fang Yujun Cui Ruifu Yang Yajun Song Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics
description	Abstract Although clinical antibiotic-resistant bacteria have attracted tremendous attention in the microbiology community, the resistant bacteria that persist in natural environments have been overlooked for a longtime. We previously proposed a new species Paramesorhizobium desertii, isolated from the soil of the Taklimakan Desert in China that is highly resistant to most β-lactam antibiotics. To identify potential β-lactamase(s) in this bacteria, we first confirmed the carbapenemase activity in the freeze–thawed supernatant of a P. desertii A-3-ET culture using the modified Hodge assay. We then identified a novel chromosome-encoded carbapenemase (PAD-1) in strain A-3-ET, using a shotgun proteomic analysis of the supernatant and genomic information. The bioinformatics analysis indicated that PAD-1 is a class A carbapenemase. Subsequent enzyme kinetic assays with purified PAD-1 confirmed its carbapenemase activity, which is similar to that of clinically significant class A carbapenemases, including BKC-1 and KPC-2. Because the location in which A-3-ET was isolated is not affected by human activity, PAD-1 is unlikely to be associated with the selection pressures exerted by modern antibiotics. This study confirmed the diversity of antibiotic-resistant determinants in the environmental resistome.
format	article
author	Ruichen Lv Jingyu Guo YanFeng Yan Rong Chen Lisheng Xiao Min Wang Nan Fang Chengxiang Fang Yujun Cui Ruifu Yang Yajun Song
author_facet	Ruichen Lv Jingyu Guo YanFeng Yan Rong Chen Lisheng Xiao Min Wang Nan Fang Chengxiang Fang Yujun Cui Ruifu Yang Yajun Song
author_sort	Ruichen Lv
title	Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics
title_short	Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics
title_full	Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics
title_fullStr	Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics
title_full_unstemmed	Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics
title_sort	characterization of a novel class a carbapenemase pad-1 from paramesorhizobium desertii a-3-et, a strain highly resistant to β-lactam antibiotics
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/13aac20497174f87aa96edd8e2638fa2
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Characterization of a novel class A carbapenemase PAD-1 from Paramesorhizobium desertii A-3-ET, a strain highly resistant to β-lactam antibiotics

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