Literature DB >> 27253479

New Delhi metallo-β-lactamase-1: structure, inhibitors and detection of producers.

Paul W Groundwater1, Sophia Xu1, Felcia Lai1, Linda Váradi1, Jinlong Tan1, John D Perry2, David E Hibbs1.   

Abstract

Since its discovery in 2008, New Delhi metallo-β-lactamase-1 (NDM-1)-producing Enterobacteriaceae have disseminated globally, facilitated predominantly by gut colonization and the spread of plasmids carrying the bla NDM-1 gene. With few effective antibiotics against NDM-1 producers, and resistance developing to those which remain, there is an urgent need to develop new treatments. To date, most drug design in this area has been focused on developing an NDM-1 inhibitor and has been aided by the wealth of structural and mechanistic information available from high resolution x-ray crystallography and molecular modeling. This review aims to summarize current knowledge regarding the detection of NDM-1 producers, the mechanism of action of NDM-1 and to highlight recent attempts toward the development of clinically useful inhibitors.

Keywords:  Enterobacteriaceae; NDM-1; New Delhi metallo-β-lactamase-1; detection; inhibitors; mechanism; substrates

Mesh:

Substances:

Year:  2016        PMID: 27253479     DOI: 10.4155/fmc-2016-0015

Source DB:  PubMed          Journal:  Future Med Chem        ISSN: 1756-8919            Impact factor:   3.808


  14 in total

1.  A Kinetic Study of the Replacement by Site Saturation Mutagenesis of Residue 119 in NDM-1 Metallo-β-Lactamase.

Authors:  Francesca Marcoccia; Paola Sandra Mercuri; Moreno Galleni; Giuseppe Celenza; Gianfranco Amicosante; Mariagrazia Perilli
Journal:  Antimicrob Agents Chemother       Date:  2018-07-27       Impact factor: 5.191

2.  Active-Site Conformational Fluctuations Promote the Enzymatic Activity of NDM-1.

Authors:  Hongmin Zhang; Guixing Ma; Yifan Zhu; Lingxiao Zeng; Ashfaq Ahmad; Changzhi Wang; Bo Pang; Huiyan Fang; Liqing Zhao; Quan Hao
Journal:  Antimicrob Agents Chemother       Date:  2018-10-24       Impact factor: 5.191

Review 3.  NDM Metallo-β-Lactamases and Their Bacterial Producers in Health Care Settings.

Authors:  Wenjing Wu; Yu Feng; Guangmin Tang; Fu Qiao; Alan McNally; Zhiyong Zong
Journal:  Clin Microbiol Rev       Date:  2019-01-30       Impact factor: 26.132

Review 4.  β-lactam/β-lactamase inhibitor combinations: an update.

Authors:  Kamaleddin H M E Tehrani; Nathaniel I Martin
Journal:  Medchemcomm       Date:  2018-08-17       Impact factor: 3.597

5.  Structure-Based Virtual Screening for the Discovery of Novel Inhibitors of New Delhi Metallo-β-lactamase-1.

Authors:  Francesca Spyrakis; Giuseppe Celenza; Francesca Marcoccia; Matteo Santucci; Simon Cross; Pierangelo Bellio; Laura Cendron; Mariagrazia Perilli; Donatella Tondi
Journal:  ACS Med Chem Lett       Date:  2017-11-26       Impact factor: 4.345

6.  Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.

Authors:  Guo-Bo Li; Jürgen Brem; Robert Lesniak; Martine I Abboud; Christopher T Lohans; Ian J Clifton; Sheng-Yong Yang; Juan-Carlos Jiménez-Castellanos; Matthew B Avison; James Spencer; Michael A McDonough; Christopher J Schofield
Journal:  Chem Commun (Camb)       Date:  2017-05-30       Impact factor: 6.222

7.  The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis.

Authors:  Han Feng; Xuehui Liu; Sheng Wang; Joy Fleming; Da-Cheng Wang; Wei Liu
Journal:  Nat Commun       Date:  2017-12-21       Impact factor: 14.919

8.  Thermokinetic profile of NDM-1 and its inhibition by small carboxylic acids.

Authors:  Qian Wang; Yuan He; Rui Lu; Wen-Ming Wang; Ke-Wu Yang; Hai Ming Fan; Yi Jin; G Michael Blackburn
Journal:  Biosci Rep       Date:  2018-04-13       Impact factor: 3.840

9.  Small Molecule Carboxylates Inhibit Metallo-β-lactamases and Resensitize Carbapenem-Resistant Bacteria to Meropenem.

Authors:  Kamaleddin H M E Tehrani; Nora C Brüchle; Nicola Wade; Vida Mashayekhi; Diego Pesce; Matthijs J van Haren; Nathaniel I Martin
Journal:  ACS Infect Dis       Date:  2020-04-03       Impact factor: 5.084

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

Authors:  Bo Ma; Chao Fang; Linshan Lu; Mingzhi Wang; Xiaoyan Xue; Ying Zhou; Mingkai Li; Yue Hu; Xiaoxing Luo; Zheng Hou
Journal:  Nat Commun       Date:  2019-08-06       Impact factor: 14.919

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