Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7

被引：54

作者：

Bergstrom, Alexander ^{[1
]}

Katko, Andrew ^{[1
]}

Adkins, Zach ^{[1
]}

Hill, Jessica ^{[1
]}

Cheng, Zishuo ^{[1
]}

Burnett, Mia ^{[1
]}

Yang, Hao ^{[1
]}

Aitha, Mahesh ^{[1
]}

Mehaffey, M. Rachel ^{[2
]}

Brodbelt, Jennifer S. ^{[2
]}

Tehrani, Kamaleddin H. M. E. ^{[3
]}

Martin, Nathaniel I. ^{[3
]}

Bonomo, Robert A. ^{[4
]}

Page, Richard C. ^{[1
]}

Tierney, David L. ^{[1
]}

Fast, Walter ^{[5
]}

Wright, Gerard D. ^{[6
,7
]}

Crowder, Michael W. ^{[1
]}

机构：

[1] Miami Univ, Dept Chem & Biochem, 650 East High St, Oxford, OH 45056 USA

[2] Univ Texas Austin, Dept Chem, Austin, TX 78712 USA

[3] Univ Utrecht, Utrecht Inst Pharmaceut Sci, Dept Chem Biol & Drug Discovery, Univ Weg 99, NL-3584 CG Utrecht, Netherlands

[4] Vet Affairs Med Ctr, Louis Stokes Cleveland Dept, Res Serv, 10701 East Blvd, Cleveland, OH USA

[5] Univ Texas Austin, Coll Pharm, Div Chem Biol & Med Chem, 107 W Dean Keeton, Austin, TX 78712 USA

[6] McMaster Univ, Michael G DeGroote Inst Infect Dis, 1280 Main St West, Hamilton, ON L8S 4L8, Canada

[7] McMaster Univ, Dept Biochem & Biomed Sci, 1280 Main St West, Hamilton, ON L8S 4L8, Canada

来源：

ACS INFECTIOUS DISEASES | 2018年 / 4卷 / 02期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

aspergillomarasmine A; metallo-beta-lactamase; NDM-1; VIM-2; IMP-7; antibiotic resistance; SPECTROSCOPIC CHARACTERIZATION; ANTIBIOTIC-RESISTANCE; MOLECULAR-MECHANISMS; MULTIDRUG-RESISTANT; STRUCTURAL BASIS; ACTIVE-SITE; INHIBITORS; NMR; COORDINATION; COBALT(II);

D O I：

10.1021/acsinfecdis.7b00106

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Metallo-beta-lactamases (MBLs) are a growing threat to the continued efficacy of beta-lactam antibiotics. Recently, aspergillomarasmine A (AMA) was identified as an MBL inhibitor, but the mode of inhibition was not fully characterized. Equilibrium dialysis and metal analysis studies revealed that 2 equiv of AMA effectively removes 1 equiv of Zn(II) from MBLs NDM-1, VIM-2, and IMP-7 when the MBL is at micromolar concentrations. Conversely, H-1 NMR studies revealed that 2 equiv of AMA remove 2 equiv of Co(II) from Co(II)-substituted NDM-1, VIM-2, and IMP-7 when the MBL/AMA are at millimolar concentrations. Our findings reveal that AMA inhibits the MBLs by removal of the active site metal ions required for beta-lactam hydrolysis among the most clinically significant MBLs.

引用

页码：135 / 145

页数：11

共 65 条

[31] Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance [J].

King, Andrew M. ;

Reid-Yu, Sarah A. ;

Wang, Wenliang ;

King, Dustin T. ;

De Pascale, Gianfranco ;

Strynadka, Natalie C. ;

Walsh, Timothy R. ;

Coombes, Brian K. ;

Wright, Gerard D. .

NATURE, 2014, 510 (7506) :503-+

[32] Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistance [J].

King, Dustin ;

Strynadka, Natalie .

PROTEIN SCIENCE, 2011, 20 (09) :1484-1491

[33] New Delhi Metallo-β-Lactamase: Structural Insights into β-Lactam Recognition and Inhibition [J].

King, Dustin T. ;

Worrall, Liam J. ;

Gruninger, Robert ;

Strynadka, Natalie C. J. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2012, 134 (28) :11362-11365

[34] Approved Drugs Containing Thiols as Inhibitors of Metallo-β-lactamases: Strategy To Combat Multidrug-Resistant Bacteria [J].

Klingler, Franca-M ;

Wichelhaus, Thomas A. ;

Frank, Denia ;

Cuesta-Bernal, Jenifer ;

El-Delik, Jasmin ;

Mueller, H. Florian ;

Sjuts, Hanno ;

Goettig, Stephan ;

Koenigs, Arno ;

Pos, Klaas M. ;

Pogoryelov, Denys ;

Proschak, Ewgenij .

JOURNAL OF MEDICINAL CHEMISTRY, 2015, 58 (08) :3626-3630

[35] The biological inorganic chemistry of zinc ions [J].

Krezel, Artur ;

Maret, Wolfgang .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2016, 611 :3-19

[36] The Challenge of Efflux-Mediated Antibiotic Resistance in Gram-Negative Bacteria [J].

Li, Xian-Zhi ;

Plesiat, Patrick ;

Nikaido, Hiroshi .

CLINICAL MICROBIOLOGY REVIEWS, 2015, 28 (02) :337-418

[37] Structural basis for the broad-spectrum inhibition of metallo-β-lactamases by thiols [J].

Lienard, Benoit M. R. ;

Garau, Gianpiero ;

Horsfall, Louise ;

Karsisiotis, Andreas I. ;

Damblon, Christian ;

Lassaux, Patricia ;

Papamicael, Cyril ;

Roberts, Gordon C. K. ;

Galleni, Moreno ;

Dideberg, Otto ;

Frere, Jean-Marie ;

Schofield, Christopher J. .

ORGANIC & BIOMOLECULAR CHEMISTRY, 2008, 6 (13) :2282-2294

[38] Overcoming differences: The catalytic mechanism of metallo-β-lactamases [J].

Meini, Maria-Rocio ;

Llarrull, Leticia I. ;

Vila, Alejandro J. .

FEBS LETTERS, 2015, 589 (22) :3419-3432

[39] B1-Metallo-β-Lactamases: Where Do We Stand? [J].

Mojica, Maria F. ;

Bonomo, Robert A. ;

Fast, Walter .

CURRENT DRUG TARGETS, 2016, 17 (09) :1029-1050

[40] Carbapenem resistance in Enterobacteriaceae: here is the storm! [J].

Nordmann, Patrice ;

Dortet, Laurent ;

Poirel, Laurent .

TRENDS IN MOLECULAR MEDICINE, 2012, 18 (05) :263-272

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