Identification and characterization of a novel metallo β-lactamase, SZM-1, in Shenzhen Bay, South China.

Identification and characterization of a novel metallo β-lactamase, SZM-1, in Shenzhen Bay, South China.
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DOI:
10.3389/fmicb.2022.996834
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发表时间:
2022
影响因子:
5.2
通讯作者:
--
中科院分区:
生物学2区
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--
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金属β-内酰胺酶(Mbls)能降解大多数临床β-内酰胺类抗生素,尤其是碳青霉烯类,对全球健康构成巨大威胁。环境微生物的研究对于评估微生物在相互关联的生境之间以及环境与人类之间传播的风险具有重要意义。在这里,我们描述了一种新的金属β-内酰胺酶,命名为SZM-1(深圳金属-β-内酰胺酶),从中国南部深圳湾地区河流沉积物中发现的Arenimonas超基因组中。系统发育分析、一级序列比较和结构模拟表明,SZM-1属于B1MBL家族,可能含有典型的双锌催化中心。进一步将编码MBLS的基因克隆到大肠杆菌TOP10中,进行Carba NP试验和药敏试验。结果表明,SZM-1菌株具有碳青霉烯酶活力,使载体对碳青霉烯类抗生素有较强的耐药性。综上所述,我们的结果对SZM-1的出现和传播提出了警告,并建议进一步监测,特别是在医院环境和临床分离株中,以确定blaSZM-1是否是可动员的抗生素耐药性。
Metallo β-Lactamases (MBLs) degrade most clinical β-lactam antibiotics, especially Carbapenem, posing a huge threat to global health. Studies on environmental MBLs are important for risk assessment of the MBLs transmission among connected habitats, and between environment and human. Here, we described a novel metallo β-Lactamases, named SZM-1 (Shenzhen metallo-β-lactamase), from an Arenimonas metagenome-assembled genome recovered from the river sediment in the Shenzhen Bay area, south China. Phylogenetic analysis, primary sequence comparison, structural modeling suggested that the SZM-1 belongs to B1 MBL family, likely harboring a typical di-zinc catalytic center. Furthermore, the gene encoding the MBLs was cloned into Escherichia coli TOP10 for Carba NP test and antimicrobial susceptibility test. The results indicated that the SZM-1 had carbapenemase activity, and conferred the carrier to increased resistance toward carbapenems. Taken together, our results raise alarms about the emergence and spread of the SZM-1, and suggest further surveillance, especially in hospital settings and clinical isolates, to determine whether blaSZM–1 is a mobilizable antibiotic resistance.
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