Fusidic Acid Resistance in Staphylococcus aureus Strains in an Interval of Ten Years (2001-2011)

2012 ◽  
Vol 32 (6) ◽  
pp. 1668-1672 ◽  
Author(s):  
Şebnem NERGİZ ◽  
Selahattin ATMACA ◽  
Tuncer ÖZEKİNCİ ◽  
Alicem TEKİN
2014 ◽  
Vol 9 (6) ◽  
pp. 737-745 ◽  
Author(s):  
Casper DJ den Heijer ◽  
Evelien ME van Bijnen ◽  
W John Paget ◽  
Ellen E Stobberingh

2007 ◽  
Vol 51 (5) ◽  
pp. 1840-1843 ◽  
Author(s):  
T. Norén ◽  
T. Åkerlund ◽  
M. Wullt ◽  
L. G. Burman ◽  
M. Unemo

ABSTRACT In silico, we identified fusA (2,067 bp) in Clostridium difficile 630. Sequencing of fusA in posttherapy fusidic acid-resistant C. difficile isolates from 12 patients with C. difficile-associated diarrhea (CDAD) identified fusA mutations, one or two nonsynonymous substitutions, or in one case a deletion of one codon associated with resistance. Five of these mutations have previously been described in fusA of fusidic acid-resistant Staphylococcus aureus, but seven were novel fusA mutations. Fusidic acid monotherapy for CDAD seemed to rapidly select conserved resistant mutants.


2003 ◽  
Vol 47 (2) ◽  
pp. 463-469 ◽  
Author(s):  
Silke Besier ◽  
Albrecht Ludwig ◽  
Volker Brade ◽  
Thomas A. Wichelhaus

2005 ◽  
Vol 49 (4) ◽  
pp. 1426-1431 ◽  
Author(s):  
Silke Besier ◽  
Albrecht Ludwig ◽  
Volker Brade ◽  
Thomas A. Wichelhaus

ABSTRACT Recent studies have shown that individual amino acid exchanges within elongation factor G (EF-G) cause fusidic acid resistance in Staphylococcus aureus. The data from the present study illustrate that the fusidic acid resistance-mediating amino acid substitutions P406L and H457Y are associated with a marked impairment of the biological fitness of S. aureus. In particular, strains producing EF-G derivatives with these mutations showed reduced growth, decreased plasma coagulase activity, and an impaired capability to compete with the isogenic wild-type strain. Second-site mutations within EF-G, such as A67T and S416F, that have been encountered in clinical fusidic acid-resistant isolates containing the amino acid exchanges P406L and H457Y, respectively, were shown not to contribute to resistance. Furthermore, the substitution A67T had no impact on the biological fitness in vitro. The exchange S416F, however, was found to function as a fitness-compensating mutation in S. aureus carrying the substitution H457Y in EF-G. In conclusion, the data presented in this report provide evidence at the molecular level that the deleterious effects of fusidic acid resistance-mediating exchanges within EF-G of S. aureus can be reduced considerably by specific compensating mutations in this target protein. This compensatory adaptation most likely plays a significant role in the stabilization of resistant bacteria within a given population.


2015 ◽  
Vol 15 (1) ◽  
Author(s):  
Fangyou Yu ◽  
Yunling Liu ◽  
Chaohui Lu ◽  
Jinnan LV ◽  
Xiuqin Qi ◽  
...  

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