Intraphagocytic Bactericidal Activity of Bacterial DNA Gyrase Inhibitors against Serratia marcescens

Chemotherapy ◽  
1984 ◽  
Vol 30 (6) ◽  
pp. 379-386 ◽  
Author(s):  
Walter H. Traub
1993 ◽  
Vol 46 (11) ◽  
pp. 1764-1766 ◽  
Author(s):  
MARCIA S. OSBURNE ◽  
WILLIAM M. MAIESE ◽  
MICHAEL GREENSTEIN

2015 ◽  
Vol 70 (9) ◽  
pp. 2576-2588 ◽  
Author(s):  
Alina Iulia Chiriac ◽  
Florian Kloss ◽  
Jonas Krämer ◽  
Cuong Vuong ◽  
Christian Hertweck ◽  
...  

RSC Advances ◽  
2015 ◽  
Vol 5 (128) ◽  
pp. 105600-105608 ◽  
Author(s):  
Long Li ◽  
Xiu Le ◽  
Ling Wang ◽  
Qiong Gu ◽  
Huihao Zhou ◽  
...  

Bacterial DNA gyrase is not expressed in eukaryotes.


1993 ◽  
Vol 214 (1) ◽  
pp. 313-317 ◽  
Author(s):  
J.F. Barrett ◽  
J.I. Bernstein ◽  
H.M. Krause ◽  
J.J. Hilliard ◽  
K.A. Ohemeng

2005 ◽  
Vol 49 (3) ◽  
pp. 1093-1100 ◽  
Author(s):  
Ruth H. Flatman ◽  
Alison J. Howells ◽  
Lutz Heide ◽  
Hans-Peter Fiedler ◽  
Anthony Maxwell

ABSTRACT We have characterized the interaction of a new class of antibiotics, simocyclinones, with bacterial DNA gyrase. Even though their structures include an aminocoumarin moiety, a key feature of novobiocin, coumermycin A1, and clorobiocin, which also target gyrase, simocyclinones behave strikingly differently from these compounds. Simocyclinone D8 is a potent inhibitor of gyrase supercoiling, with a 50% inhibitory concentration lower than that of novobiocin. However, it does not competitively inhibit the DNA-independent ATPase reaction of GyrB, which is characteristic of other aminocoumarins. Simocyclinone D8 also inhibits DNA relaxation by gyrase but does not stimulate cleavage complex formation, unlike quinolones, the other major class of gyrase inhibitors; instead, it abrogates both Ca2+- and quinolone-induced cleavage complex formation. Binding studies suggest that simocyclinone D8 interacts with the N-terminal domain of GyrA. Taken together, our results demonstrate that simocyclinones inhibit an early step of the gyrase catalytic cycle by preventing binding of the enzyme to DNA. This is a novel mechanism for a gyrase inhibitor and presents new possibilities for antibacterial drug development.


2011 ◽  
Vol 2 (4) ◽  
pp. 289-292 ◽  
Author(s):  
Marie H. Foss ◽  
Katherine A. Hurley ◽  
Nohemy A. Sorto ◽  
Laura L. Lackner ◽  
Kelsey M. Thornton ◽  
...  

2017 ◽  
Vol 27 (5) ◽  
pp. 1162-1168 ◽  
Author(s):  
Hülya Karaca Gençer ◽  
Serkan Levent ◽  
Ulviye Acar Çevik ◽  
Yusuf Özkay ◽  
Sinem Ilgın
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