Prevalence of Plasmid-Mediated Fosfomycin Resistance Gene fosA3 Among CTX-M-Producing Escherichia coli Isolates from Chickens in China

2017 ◽  
Vol 14 (4) ◽  
pp. 210-218 ◽  
Author(s):  
Wei Jiang ◽  
Shuai Men ◽  
Linghan Kong ◽  
Suzhen Ma ◽  
Yongqiang Yang ◽  
...  
2012 ◽  
Vol 68 (4) ◽  
pp. 766-770 ◽  
Author(s):  
J. Hou ◽  
X. Yang ◽  
Z. Zeng ◽  
L. Lv ◽  
T. Yang ◽  
...  

2015 ◽  
Vol 362 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Jing-yi Zhao ◽  
Yuan-qi Zhu ◽  
Yan-nian Li ◽  
Xiao-dong Mu ◽  
Li-ping You ◽  
...  

2020 ◽  
Vol Volume 13 ◽  
pp. 1273-1279 ◽  
Author(s):  
Ying Huang ◽  
Qingqing Lin ◽  
Qiaoli Zhou ◽  
Luchao Lv ◽  
Miao Wan ◽  
...  

2017 ◽  
Vol 61 (9) ◽  
Author(s):  
Xiu-Mei Wang ◽  
Zhimin Dong ◽  
Stefan Schwarz ◽  
Yao Zhu ◽  
Xin Hua ◽  
...  

ABSTRACT Thirty-nine fosfomycin-resistant Escherichia coli isolates carrying fosA3 were obtained from pigs, chickens, dairy cows, and staff in four northeastern provinces of China between June 2015 and April 2016. The fosA3 gene was colocated with bla CTX-M genes on conjugative plasmids of the incompatibility groups IncN (n = 12), IncN-F33:A−:B−(n = 2), IncF33:A−:B−(n = 14), IncF14:A−:B−(n = 2), and IncI1/sequence type 136 (ST136) (n = 9). Four different genetic contexts of fosA3 were detected among the 39 E. coli isolates. Three potential epidemic plasmids circulated among E. coli strains from this region.


2013 ◽  
Vol 19 (6) ◽  
pp. 477-482 ◽  
Author(s):  
Natsumi Sato ◽  
Kumiko Kawamura ◽  
Kunihiko Nakane ◽  
Jun-Ichi Wachino ◽  
Yoshichika Arakawa

2017 ◽  
Vol 61 (11) ◽  
Author(s):  
Erik H. Klontz ◽  
Adam D. Tomich ◽  
Sebastian Günther ◽  
Justin A. Lemkul ◽  
Daniel Deredge ◽  
...  

ABSTRACT Fosfomycin exhibits broad-spectrum antibacterial activity and is being reevaluated for the treatment of extensively drug-resistant pathogens. Its activity in Gram-negative organisms, however, can be compromised by expression of FosA, a metal-dependent transferase that catalyzes the conjugation of glutathione to fosfomycin, rendering the antibiotic inactive. In this study, we solved the crystal structures of two of the most clinically relevant FosA enzymes: plasmid-encoded FosA3 from Escherichia coli and chromosomally encoded FosA from Klebsiella pneumoniae (FosAKP). The structure, molecular dynamics, catalytic activity, and fosfomycin resistance of FosA3 and FosAKP were also compared to those of FosA from Pseudomonas aeruginosa (FosAPA), for which prior crystal structures exist. E. coli TOP10 transformants expressing FosA3 and FosAKP conferred significantly greater fosfomycin resistance (MIC, >1,024 μg/ml) than those expressing FosAPA (MIC, 16 μg/ml), which could be explained in part by the higher catalytic efficiencies of the FosA3 and FosAKP enzymes. Interestingly, these differences in enzyme activity could not be attributed to structural differences at their active sites. Instead, molecular dynamics simulations and hydrogen-deuterium exchange experiments with FosAKP revealed dynamic interconnectivity between its active sites and a loop structure that extends from the active site of each monomer and traverses the dimer interface. This dimer interface loop is longer and more extended in FosAKP and FosA3 than in FosAPA, and kinetic analyses of FosAKP and FosAPA loop-swapped chimeric enzymes highlighted its importance in FosA activity. Collectively, these data yield novel insights into fosfomycin resistance that could be leveraged to develop new strategies to inhibit FosA and potentiate fosfomycin activity.


1997 ◽  
Vol 41 (2) ◽  
pp. 314-318 ◽  
Author(s):  
E Hannecart-Pokorni ◽  
F Depuydt ◽  
L de wit ◽  
E van Bossuyt ◽  
J Content ◽  
...  

The amikacin resistance gene aac(6')-Im [corrected] from Citrobacter freundii Cf155 encoding an aminoglycoside 6'-N-acetyltransferase was characterized. The gene was identified as a coding sequence of 521 bp located down-stream from the 5' conserved segment of an integron. The sequence of this aac(6')-Im [corrected] gene corresponded to a protein of 173 amino acids which possessed 64.2% identity in a 165-amino-acid overlap with the aac(6')-Ia gene product (F.C. Tenover, D. Filpula, K.L. Phillips, and J. J. Plorde, J. Bacteriol. 170:471-473, 1988). By using PCR, the aac(6')-Im [corrected] gene could be detected in 8 of 86 gram-negative clinical isolates from two Belgian hospitals, including isolates of Citrobacter, Klebsiella spp., and Escherichia coli. PCR mapping of the aac(6')-Im [corrected] gene environment in these isolates indicated that the gene was located within a sulI-type integron; the insert region is 1,700 bases long and includes two genes cassettes, the second being ant (3")-Ib.


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