Antibiotic resistance
Carbapenamase
KPC-2
NMR
β-Lactamase
Journal
Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
22
09
2018
accepted:
11
12
2018
pubmed:
16
12
2018
medline:
20
8
2019
entrez:
16
12
2018
Statut:
ppublish
Résumé
The ever-increasing occurrence of antibiotic resistance presents a major threat to public health. Specifically, resistance conferred by β-lactamases places the efficacy of currently available antibiotics at risk. Klebsiella pneumoniae carbapenemase-2 (KPC-2) is a β-lactamase that enables carbapenem resistance and represents a clear and present danger to global public health. In order to combat bacterial infections harboring KPC-2 expression, inhibitors with improved potency need to be developed. Although the structure of KPC-2 has been solved by X-ray crystallography, NMR provides the unique opportunity to study the structure and dynamics of flexible loop regions in solution. Here we report the
Identifiants
pubmed: 30552637
doi: 10.1007/s12104-018-9866-8
pii: 10.1007/s12104-018-9866-8
pmc: PMC6440833
mid: NIHMS1004641
doi:
Substances chimiques
Carbon Isotopes
0
Nitrogen Isotopes
0
Nitrogen-15
0
Protons
0
beta-Lactamases
EC 3.5.2.6
beta-lactamase KPC-2, Klebsiella pneumoniae
EC 3.5.2.6
Carbon-13
FDJ0A8596D
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Pagination
139-142Subventions
Organisme : NIAID NIH HHS
ID : R01 AI100560
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI114508
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI072219
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI063517
Pays : United States
Organisme : BLRD VA
ID : I01 BX001974
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM128595
Pays : United States
Références
Barnes MD, Winkler ML, Taracila MA et al (2017) Klebsiella pneumoniae Carbapenemase-2 (KPC-2), Substitutions at Ambler position Asp179, and resistance to ceftazidime-avibactam: unique antibiotic-resistant phenotypes emerge from β-lactamase protein engineering. MBio 8:e00528–e00517. https://doi.org/10.1128/mBio.00528-17
doi: 10.1128/mBio.00528-17
Blair JMA, Webber MA, Baylay AJ et al (2015) Molecular mechanisms of antibiotic resistance. Nat Rev Micro 13:42–51. https://doi.org/10.1038/nrmicro3380
doi: 10.1038/nrmicro3380
Coleman K (2011) Diazabicyclooctanes (DBOs): a potent new class of non-β-lactam β-lactamase inhibitors. Curr Opin Microbiol 14:550–555. https://doi.org/10.1016/j.mib.2011.07.026
doi: 10.1016/j.mib.2011.07.026
Delaglio F, Grzesiek S, Vuister GW et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
doi: 10.1007/BF00197809
Ehmann DE, Jahić H, Ross PL et al (2013) Kinetics of Avibactam Inhibition against Class A, C, and D β-Lactamases. J Biol Chem 288:27960–27971. https://doi.org/10.1074/jbc.M113.485979
doi: 10.1074/jbc.M113.485979
Ke W, Bethel CR, Thomson JM et al (2007) Crystal structure of KPC-2: insights into carbapenemase activity in class A beta-lactamases. Biochemistry 46:5732–5740. https://doi.org/10.1021/bi700300u
doi: 10.1021/bi700300u
Krishnan NP, Nguyen NQ, Papp-Wallace KM et al (2015) Inhibition of Klebsiella β-Lactamases (SHV-1 and KPC-2) by Avibactam: a structural study. PLoS ONE 10:e0136813. https://doi.org/10.1371/journal.pone.0136813
doi: 10.1371/journal.pone.0136813
Lee W, Tonelli M, Markley JL (2015) NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy. Bioinformatics 31:1325–1327. https://doi.org/10.1093/bioinformatics/btu830
doi: 10.1093/bioinformatics/btu830
Levitt PS, Papp-Wallace KM, Taracila MA et al (2012) Exploring the role of a conserved class A residue in the Ω-Loop of KPC-2 β-lactamase: a mechanism for ceftazidime hydrolysis. J Biol Chem 287:31783–31793. https://doi.org/10.1074/jbc.M112.348540
doi: 10.1074/jbc.M112.348540
Majiduddin FK, Materon IC, Palzkill TG (2002) Molecular analysis of beta-lactamase structure and function. Int J Med Microbiol 292:127–137. https://doi.org/10.1078/1438-4221-00198
doi: 10.1078/1438-4221-00198
Munoz-Price LS, Poirel L, Bonomo RA et al (2013) Clinical epidemiology of the global expansion of Klebsiella pneumoniae carbapenemases. Lancet Infect Dis 13:785–796. https://doi.org/10.1016/S1473-3099(13)70190-7
doi: 10.1016/S1473-3099(13)70190-7
Nordmann P, Cuzon G, Naas T (2009) The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria. Lancet Infect Dis 9:228–236. https://doi.org/10.1016/S1473-3099(09)70054-4
doi: 10.1016/S1473-3099(09)70054-4
Palzkill T, Le QQ, Venkatachalam KV et al (1994) Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of beta-lactamase. Mol Microbiol 12:217–229
doi: 10.1111/j.1365-2958.1994.tb01011.x
Papp-Wallace KM, Bethel CR, Distler AM et al (2010) Inhibitor resistance in the KPC-2 beta-lactamase, a preeminent property of this class A beta-lactamase. Antimicrob Agents Chemother 54:890–897. https://doi.org/10.1128/AAC.00693-09
doi: 10.1128/AAC.00693-09
Papp-Wallace KM, Winkler ML, Taracila MA, Bonomo RA (2015) Variants of β-lactamase KPC-2 that are resistant to inhibition by avibactam. Antimicrob Agents Chemother 59:3710–3717. https://doi.org/10.1128/AAC.04406-14
doi: 10.1128/AAC.04406-14
Raquet X, Lamotte-Brasseur J, Fonzé E et al (1994) TEM beta-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis. J Mol Biol 244:625–639. https://doi.org/10.1006/jmbi.1994.1756
doi: 10.1006/jmbi.1994.1756
Shapiro AB (2017) Kinetics of Sulbactam Hydrolysis by β-Lactamases, and Kinetics of β-Lactamase Inhibition by Sulbactam. Antimicrob Agents Chemother 61:e01612–e01617. https://doi.org/10.1128/AAC.01612-17
doi: 10.1128/AAC.01612-17
Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213–223. https://doi.org/10.1007/s10858-009-9333-z
doi: 10.1007/s10858-009-9333-z