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

[51] Characterization of Purified New Delhi Metallo-β-lactamase-1 [J].

Thomas, Pei W. ;

Zheng, Min ;

Wu, Shanshan ;

Guo, Hua ;

Liu, Dali ;

Xu, Dingguo ;

Fast, Walter .

BIOCHEMISTRY, 2011, 50 (46) :10102-10113

[52] Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-β-lactamase [J].

Toney, JH ;

Hammond, GG ;

Fitzgerald, PMD ;

Sharma, N ;

Balkovec, JM ;

Rouen, GP ;

Olson, SH ;

Hammond, ML ;

Greenlee, ML ;

Gao, YD .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (34) :31913-31918

[53] Molecular mechanisms of antimicrobial tolerance and resistance in bacterial and fungal biofilms [J].

Van Acker, Heleen ;

Van Dijck, Patrick ;

Coenye, Tom .

TRENDS IN MICROBIOLOGY, 2014, 22 (06) :326-333

[54]

VANWART HE, 1988, METHOD ENZYMOL, V158, P95

[55] ENZYMATICALLY INACTIVE, EXCHANGE-INERT CO(III)-CARBOXYPEPTIDASE-A - ROLE OF INNER SPHERE COORDINATION IN PEPTIDE AND ESTER CATALYSIS [J].

VANWART, HE ;

VALLEE, BL .

BIOCHEMISTRY, 1978, 17 (16) :3385-3394

[56] The identification of new metallo-β-lactamase inhibitor leads from fragment-based screening [J].

Vella, Peter ;

Hussein, Waleed M. ;

Leung, Eleanor W. W. ;

Clayton, Daniel ;

Ollis, David L. ;

Mitic, Natasa ;

Schenk, Gerhard ;

McGeary, Ross P. .

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2011, 21 (11) :3282-3285

[57] Aspergillomarasmine A, an Inhibitor of Bacterial Metallo-β-Lactamases Conferring blaNDM and blaVIM Resistance [J].

von Nussbaum, Franz ;

Schiffer, Guido .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2014, 53 (44) :11696-11698

[58] Metallo-β-lactamases:: the quiet before the storm? [J].

Walsh, TR ;

Toleman, MA ;

Poirel, L ;

Nordmann, P .

CLINICAL MICROBIOLOGY REVIEWS, 2005, 18 (02) :306-+

[59] EXCHANGE-INERT METAL-IONS AS PROBES OF ENZYME STRUCTURE-FUNCTION-RELATIONSHIPS - COBALT(III), COBALT(II), AND ZINC(II) AZOPHENOL COMPLEXES AS MODELS FOR ENZYME AZOTYROSINE COMPLEXES [J].

WHITE, WI ;

LEGG, JI .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1975, 97 (14) :3937-3941

[60] Substrate-activated zinc binding of metallo-β-lactamases -: Physiological importance of the mononuclear enzymes [J].

Wommer, S ;

Rival, S ;

Heinz, U ;

Galleni, M ;

Frère, JM ;

Franceschini, N ;

Amicosante, G ;

Rasmussen, B ;

Bauer, R ;

Adolph, HW .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (27) :24142-24147

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