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Tytuł pozycji:

Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.

Tytuł:
Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
Autorzy:
Krucinska J; Department of Pharmaceutical Sciences, University of Connecticut, 69N. Eagleville Rd., Storrs, CT, 06269, USA.
Lombardo MN; Department of Pharmaceutical Sciences, University of Connecticut, 69N. Eagleville Rd., Storrs, CT, 06269, USA.
Erlandsen H; Center for Open Research Resources & Equipment (COR2E), University of Connecticut, 91N. Eagleville Rd., Storrs, CT, 06269, USA.
Estrada A; Department of Pharmaceutical Sciences, University of Connecticut, 69N. Eagleville Rd., Storrs, CT, 06269, USA.
Si D; Department of Pharmaceutical Sciences, University of Connecticut, 69N. Eagleville Rd., Storrs, CT, 06269, USA.
Viswanathan K; Department of Pharmaceutical Sciences, University of Connecticut, 69N. Eagleville Rd., Storrs, CT, 06269, USA.
Wright DL; Department of Pharmaceutical Sciences, University of Connecticut, 69N. Eagleville Rd., Storrs, CT, 06269, USA. .
Źródło:
Communications biology [Commun Biol] 2022 May 13; Vol. 5 (1), pp. 459. Date of Electronic Publication: 2022 May 13.
Typ publikacji:
Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, N.I.H., Extramural
Język:
English
Imprint Name(s):
Original Publication: London, United Kingdom : Nature Publishing Group UK, [2018]-
MeSH Terms:
Folic Acid Antagonists*/chemistry
Folic Acid Antagonists*/metabolism
Folic Acid Antagonists*/pharmacology
Trimethoprim Resistance*/genetics
Escherichia coli/genetics ; Escherichia coli/metabolism ; Folic Acid/analogs & derivatives ; Plasmids/genetics ; Tetrahydrofolate Dehydrogenase/chemistry ; Tetrahydrofolate Dehydrogenase/genetics ; Tetrahydrofolate Dehydrogenase/metabolism
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Grant Information:
R01 AI104841 United States AI NIAID NIH HHS; P30 GM133893 United States GM NIGMS NIH HHS; P30 GM133894 United States GM NIGMS NIH HHS
Substance Nomenclature:
0 (Folic Acid Antagonists)
4033-27-6 (dihydrofolate)
935E97BOY8 (Folic Acid)
EC 1.5.1.3 (Tetrahydrofolate Dehydrogenase)
Entry Date(s):
Date Created: 20220513 Date Completed: 20220517 Latest Revision: 20220716
Update Code:
20240105
PubMed Central ID:
PMC9106665
DOI:
10.1038/s42003-022-03384-y
PMID:
35562546
Czasopismo naukowe
Two plasmid-encoded dihydrofolate reductase (DHFR) isoforms, DfrA1 and DfrA5, that give rise to high levels of resistance in Gram-negative bacteria were structurally and biochemically characterized to reveal the mechanism of TMP resistance and to support phylogenic groupings for drug development against antibiotic resistant pathogens. Preliminary screening of novel antifolates revealed related chemotypes that showed high levels of inhibitory potency against Escherichia coli chromosomal DHFR (EcDHFR), DfrA1, and DfrA5. Kinetics and biophysical analysis, coupled with crystal structures of trimethoprim bound to EcDHFR, DfrA1 and DfrA5, and two propargyl-linked antifolates (PLA) complexed with EcDHFR, DfrA1 and DfrA5, were determined to define structural features of the substrate binding pocket and guide synthesis of pan-DHFR inhibitors.
(© 2022. The Author(s).)
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