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New delhi metallo

Shui Liu, Yonglin Zhou, Xiaodi Niu, Tingting Wang, Jiyun Li, Zhongjie Liu, Jianfeng Wang, Shusheng Tang, Yang Wang, Xuming Deng
The emergence of plasmid-mediated New Delhi metallo-β-lactamase-1 (NDM-1) in carbapenem-resistant Gram-negative pathogens is an increasing clinical threat. Here we report the discovery of an NDM-1 inhibitor, magnolol, through enzyme inhibition screening. We showed that magnolol significantly inhibited NDM enzyme activity (IC50  = 6.47 µg/mL), and it restored the activity of meropenem against Escherichia coli ZC-YN3, an NDM-1-producing E. coli isolate, in in vitro antibacterial activity assays. Magnolol lacked direct antibacterial activity, but compared with meropenem alone, it reduced the MICs of meropenem against E...
December 2018: Cell Death Discovery
Zhihai Liu, Jiyun Li, Xiaoming Wang, Dejun Liu, Yuebin Ke, Yang Wang, Jianzhong Shen
The spread of carbapenem-resistant Enterobacteriaceae (CRE) mediated by New Delhi metallo-β-lactamase (NDM) poses a serious challenge to clinicians and has become a major public health concern. NDM has been evolving into variants that possess different hydrolysis activity toward antibiotics, so as to affect treatment strategy. In addition, very few studies on NDM variants have focused on animal-derived bacterial isolates. Our study reports a novel NDM variant, NDM-20, in an isolate of Escherichia coli CCD1 recovered from the food animal swine in China...
2018: Frontiers in Microbiology
Qian Wang, Yuan He, Rui Lu, Wen-Ming Wang, Ke-Wu Yang, Hai Ming Fan, Yi Jin, G Michael Blackburn
The New Delhi metallo-β-lactamase (NDM-1) is an important clinical target for antimicrobial research, but there are insufficient clinically useful inhibitors and the details of NDM-1 enzyme catalysis remain unclear. The aim of this work is to provide a thermodynamic profile of NDM-1 catalysed hydrolysis of β-lactams using an isothermal titration calorimetry (ITC) approach and to apply this new method to the identification of new low-molecular-weight dicarboxylic acid inhibitors. The results reveal that hydrolysis of penicillin G and imipenem by NDM-1 share the same thermodynamic features with a significant intrinsic enthalpy change and the release of one proton into solution, while NDM-1 hydrolysis of cefazolin exhibits a different mechanism with a smaller enthalpy change and the release of two protons...
March 5, 2018: Bioscience Reports
Maria Giufrè, Giulia Errico, Marisa Accogli, Monica Monaco, Laura Villa, Maria Antonietta Distasi, Tito Del Gaudio, Annalisa Pantosti, Alessandra Carattoli, Marina Cerquetti
The emergence of carbapenemase-producing Enterobacteriaceae (CPE) is a critical concern worldwide. In Italy, CPE isolates are very frequent with the KPC types strongly predominant whereas the New Delhi metallo-β-lactamase (NDM) enzymes are extremely rare. In this study, we report the first detection of NDM-5-producing Escherichia coli sequence type (ST) 167 isolates from two patients with urinary tract infection (Ec001and Ec002 from urines) including one with colonization (Ec003 from faeces) admitted to the same hospital in 2017 two months apart...
February 28, 2018: International Journal of Antimicrobial Agents
Abid Ali, Mohd W Azam, Asad U Khan
New Delhi metallo β-lactamase-1 is one of the carbapenemases, causing hydrolysis of almost all β-lactamase antibiotics. Seventeen different NDM variants have been reported so far, they varied in their sequences either by single or multiple amino acid substitutions. Hence, it is important to understand its structural and functional relation. In the earlier studies role of active site residues has been studied but non-active site residues has not studied in detail. Therefore, we have initiated to further comprehend its structure and function relation by mutating some of its non-active site residues...
February 15, 2018: International Journal of Biological Macromolecules
Juan Duan, Chuncai Hu, Jiafan Guo, Lianxian Guo, Jia Sun, Zuguo Zhao
The mechanism of substrate hydrolysis of New Delhi metallo-β-lactamase 1 (NDM-1) has been reported, but the process in which NDM-1 captures and transports the substrate into its active center remains unknown. In this study, we investigated the process of the substrate entry into the NDM-1 activity center through long unguided molecular dynamics simulations using meropenem as the substrate. A total of 550 individual simulations were performed, each of which for 200 ns, and 110 of them showed enzyme-substrate binding events...
February 14, 2018: Physical Chemistry Chemical Physics: PCCP
Siew Mun Liew, Ganeswrei Rajasekaram, Savithri D Puthucheary, Kek Heng Chua
OBJECTIVES: The increasing incidence of carbapenem-resistant Pseudomonas aeruginosa along with the discovery of novel metallo-β-lactamases (MBLs) is of concern. In this study, the isolation of Malaysian MBL-producing P. aeruginosa clinical strains was investigated. METHODS: Fifty-three P. aeruginosa clinical strains were isolated from different patients in Sultanah Aminah Hospital, Johor Bahru, Malaysia in 2015. Antimicrobial susceptibility test was conducted. Minimum inhibitory concentrations (MICs) of imipenem and meropenem were determined by Etest...
February 9, 2018: Journal of Global Antimicrobial Resistance
Nian-Zhi Ning, Xiong Liu, Fanghong Chen, Peng Zhou, Lihong Hu, Jian Huang, Zhan Li, Jie Huang, Tao Li, Hui Wang
The emergence and spread of carbapenemase in Gram-negative pathogens poses an enormous threat to global public health. New Delhi metallo-β-lactamase-1 (NDM-1) inactivates nearly every class of β-lactam antibiotics, including carbapenem; however, there is no clinically useful NDM-1 inhibitor. Embelin, an important ingredient in traditional herbal medicine, has anti-tumor effects. The current study is the first to discover and examine the inhibitory activity of embelin against β-lactamase NDM-1. The IC50 of embelin was 2...
2018: Frontiers in Microbiology
Michael J Ray, Michael Y Lin, Angela S Tang, M Allison Arwady, Mary Alice Lavin, Erica Runningdeer, Dejan Jovanov, William E Trick
Background: In 2013, New Delhi metallo-β-lactamase-producing Escherichia coli, a type of carbapenem-resistant Enterobacteriaceae uncommon in the United States, was identified in a tertiary care hospital (Hospital A) in northeastern Illinois. The outbreak was traced to a contaminated duodenoscope. Patient-sharing patterns can be described through social network analysis and ego networks, which could be used to identify hospitals most likely to accept patients from a hospital with an outbreak...
February 3, 2018: Clinical Infectious Diseases: An Official Publication of the Infectious Diseases Society of America
Yi Li, Qiao-Ling Sun, Yingbo Shen, Yangjunna Zhang, Jun-Wen Yang, Ling-Bin Shu, Hong-Wei Zhou, Yang Wang, Bing Wang, Rong Zhang, Shaolin Wang, Zhangqi Shen
The global spread of carbapenem-resistant Enterobacteriaceae (CRE) is one of the most severe threats to human health in a clinical setting. The recent emergence of plasmid-mediated colistin resistance gene mcr-1 amongst CRE strains greatly compromises the use of colistin as a last resort for the treatment of infections caused by CRE. This study aimed to understand the current epidemiological trends and characteristics of CRE from a large hospital in Henan, the most populous province in China. From 2014--2016, a total of 7,249 Enterobacteriaceae isolates were collected from clinical samples, among which 18...
January 31, 2018: Journal of Clinical Microbiology
Runming Wang, Tsz-Pui Lai, Peng Gao, Hongmin Zhang, Pak-Leung Ho, Patrick Chiu-Yat Woo, Guixing Ma, Richard Yi-Tsun Kao, Hongyan Li, Hongzhe Sun
Drug-resistant superbugs pose a huge threat to human health. Infections by Enterobacteriaceae producing metallo-β-lactamases (MBLs), e.g., New Delhi metallo-β-lactamase 1 (NDM-1) are very difficult to treat. Development of effective MBL inhibitors to revive the efficacy of existing antibiotics is highly desirable. However, such inhibitors are not clinically available till now. Here we show that an anti-Helicobacter pylori drug, colloidal bismuth subcitrate (CBS), and related Bi(III) compounds irreversibly inhibit different types of MBLs via the mechanism, with one Bi(III) displacing two Zn(II) ions as revealed by X-ray crystallography, leading to the release of Zn(II) cofactors...
January 30, 2018: Nature Communications
Sha Liu, Li Jing, Zhu-Jun Yu, Chengyong Wu, Yongxiang Zheng, En Zhang, Qiang Chen, Yamei Yu, Li Guo, Yong Wu, Guo-Bo Li
The emergence and global spread of metallo-β-lactamase (MBL) mediated resistance to almost all β-lactam antibacterials poses a serious threat to public health. Since no clinically useful MBL inhibitors have been reported, there is an urgent need to develop new potent broad-spectrum MBL inhibitors effective against antibacterial resistance. Herein, we synthesized a set of 2-substituted ((S)-3-mercapto-2-methylpropanamido) acetic acid derivatives, some of which displayed potent inhibition with high ligand efficiency to the clinically relevant MBL subtypes, Verona Integron-encoded MBL (VIM)-2 and New Delhi MBL (NDM)-1...
January 11, 2018: European Journal of Medicinal Chemistry
Francesca Spyrakis, Giuseppe Celenza, Francesca Marcoccia, Matteo Santucci, Simon Cross, Pierangelo Bellio, Laura Cendron, Mariagrazia Perilli, Donatella Tondi
Bacterial resistance has become a worldwide concern after the emergence of metallo-β-lactamases (MBLs). They represent one of the major mechanisms of bacterial resistance against beta-lactam antibiotics. Among MBLs, New Delhi metallo-β-lactamase-1 NDM-1, the most prevalent type, is extremely efficient in inactivating nearly all-available antibiotics including last resort carbapenems. No inhibitors for NDM-1 are currently available in therapy, making the spread of NDM-1 producing bacterial strains a serious menace...
January 11, 2018: ACS Medicinal Chemistry Letters
Xia-Wei Jiang, Hong Cheng, Ying-Yi Huo, Lin Xu, Yue-Hong Wu, Wen-Hong Liu, Fang-Fang Tao, Xin-Jie Cui, Bei-Wen Zheng
Metallo-β-lactamases (MBLs) are a group of enzymes that can inactivate most commonly used β-lactam-based antibiotics. Among MBLs, New Delhi metallo-β-lactamase-1 (NDM-1) constitutes an urgent threat to public health as evidenced by its success in rapidly disseminating worldwide since its first discovery. Here we report the biochemical and genetic characteristics of a novel MBL, ElBla2, from the marine bacterium Erythrobacter litoralis HTCC 2594. This enzyme has a higher amino acid sequence similarity to NDM-1 (56%) than any previously reported MBL...
January 16, 2018: Scientific Reports
Folkert Reck, Alun Bermingham, Johanne Blais, Vladimir Capka, Taryn Cariaga, Anthony Casarez, Richard Colvin, Charles R Dean, Alex Fekete, Wanben Gong, Ellie Growcott, Hongqiu Guo, Adriana K Jones, Cindy Li, Fengxia Li, Xiaodong Lin, Mika Lindvall, Sara Lopez, David McKenney, Louis Metzger, Heinz E Moser, Ramadevi Prathapam, Dita Rasper, Patrick Rudewicz, Vijay Sethuraman, Xiaoyu Shen, Jacob Shaul, Robert L Simmons, Kyuto Tashiro, Dazhi Tang, Meiliana Tjandra, Nancy Turner, Tsuyoshi Uehara, Charles Vitt, Steven Whitebread, Aregahegn Yifru, Xu Zang, Qingming Zhu
Metallo-β-lactamases (MBLs), such as New Delhi metallo-β-lactamase (NDM-1) have spread world-wide and present a serious threat. Expression of MBLs confers resistance in Gram-negative bacteria to all classes of β-lactam antibiotics, with the exception of monobactams, which are intrinsically stable to MBLs. However, existing first generation monobactam drugs like aztreonam have limited clinical utility against MBL-expressing strains because they are impacted by serine β-lactamases (SBLs), which are often co-expressed in clinical isolates...
January 4, 2018: Bioorganic & Medicinal Chemistry Letters
Ibrahim A Al-Zahrani, Bander A Alsiri
To identify the prevalence of carbapenem-resistant Klebsiella pneumoniae (CRKP) and the most common types of cabapenemases among CRKP in the Southern (Asir) province hospitals, Saudi Arabia. Methods: The cross-sectional study was conducted between late April and September in 2015. A total of 54 Klebsiella pneumoniae (K. pneumoniae) isolates with reduced sensitivity to carbapenems were obtained from various clinical specimens of the 2 largest hospitals in the Southern province. Minimum inhibitory concentrations (MICs) of carbapenems were confirmed using E-test...
January 2018: Saudi Medical Journal
Farzaneh Firoozeh, Zeinab Mahluji, Ehsaneh Shams, Ahmad Khorshidi, Mohammad Zibaei
Background and Objectives: New Delhi metallo-ß-lactamase (NDM) is a newly emerging metallo-ß-lactamases, which can destroy all β-lactams including carbapenems. Therefore, this study aimed at evaluating New Delhi metallo-ß-lactamase-1-production in clinical isolates of Klebsiella pneumoniae in Kashan, Iran. Materials and Methods: In a cross-sectional study, 181 K. pneumoniae isolates were collected from clinical samples of patients, who referred to Shahid Beheshi hospital in Kashan during November 2013 and October 2014...
October 2017: Iranian Journal of Microbiology
M J Hasan, S M Shamsuzzaman
BACKGROUND: The adeB gene in Acinetobacter baumannii regulates the bacterial internal drug efflux pump that plays a significant role in drug resistance. The aim of our study was to determine the occurrence of adeB gene in multidrug resistant and New Delhi metallo-beta-lactamase-1 (NDM- 1) gene in imipenem resistant Acinetobacter baumannii isolated from wound swab samples in a tertiary care hospital of Bangladesh. METHODS: A total of 345 wound swab samples were tested for bacterial pathogens...
December 2017: Malaysian Journal of Pathology
Han Feng, Xuehui Liu, Sheng Wang, Joy Fleming, Da-Cheng Wang, Wei Liu
New Delhi metallo-β-lactamases (NDMs), the recent additions to metallo-β-lactamases (MBLs), pose a serious public health threat due to its highly efficient hydrolysis of β-lactam antibiotics and rapid worldwide dissemination. The MBL-hydrolyzing mechanism for carbapenems is less studied than that of penicillins and cephalosporins. Here, we report crystal structures of NDM-1 in complex with hydrolyzed imipenem and meropenem, at resolutions of 1.80-2.32 Å, together with NMR spectra monitoring meropenem hydrolysis...
December 21, 2017: Nature Communications
Ágnes Sonnevend, Nour Yahfoufi, Akela Ghazawi, Wafaa Jamal, Vincent Rotimi, Tibor Pál
Carbapenem-resistant Enterobacteriaceae encountered in countries of the Arabian Peninsula usually produce OXA-48-like and New Delhi metallo-beta-lactamases (NDM) carbapenemases. However, a temporary increase in VIM-4-producing, clonally unrelated Enterobacteriaceae strains was described earlier in a Kuwaiti hospital. We investigated the genetic support of blaVIM-4 in six Klebsiella pneumoniae strains, one Escherichia coli, and one Enterobacter cloacae strain and compared it to that of VIM-4-producing isolates from other countries of the region...
2017: Infection and Drug Resistance
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