scholarly journals Aph(3′)-IIc, an Aminoglycoside Resistance Determinant from Stenotrophomonas maltophilia

2006 ◽  
Vol 51 (1) ◽  
pp. 359-360 ◽  
Author(s):  
Aki Okazaki ◽  
Matthew B. Avison

ABSTRACT We report the characterization of an intrinsic, chromosomally carried aph(3′)-IIc gene from Stenotrophomonas maltophilia clinical isolate K279a, encoding an aminoglycoside phosphotransferase enzyme that significantly increases MICs of kanamycin, neomycin, butirosin, and paromomycin when expressed in Escherichia coli. Disruption of aph(3′)-IIc in K279a results in decreased MICs of these drugs.

2020 ◽  
Vol Volume 13 ◽  
pp. 561-566
Author(s):  
Yoko Takayama ◽  
Tsuyoshi Sekizuka ◽  
Hidehito Matsui ◽  
Yuzuru Adachi ◽  
Ryotaro Eda ◽  
...  

1999 ◽  
Vol 43 (10) ◽  
pp. 2366-2371 ◽  
Author(s):  
Thierry Lambert ◽  
Marie-Cécile Ploy ◽  
François Denis ◽  
Patrice Courvalin

ABSTRACT The aac(6′)-Iz gene of Stenotrophomonas maltophilia BM2690 encoding an aminoglycoside 6′-N-acetyltransferase was characterized. The gene was identified as a coding sequence of 462 bp corresponding to a protein with a calculated mass of 16,506 Da, a value in good agreement with that of ca. 16,000 found by in vitro coupled transcription-translation. Analysis of the deduced amino acid sequence indicated that the protein was a member of the major subfamily of aminoglycoside 6′-N-acetyltransferases. The enzyme conferred resistance to amikacin but not to gentamicin, indicating that it was an AAC(6′) of type I. The open reading frame upstream from the aac(6′)-Izgene was homologous to the fprA gene of Myxococcus xanthus (61% identity), which encodes a putative pyridoxine (pyridoxamine) 5′-phosphate oxidase. Pulsed-field gel electrophoresis of total DNA from BM2690 and S. maltophilia ATTC 13637 digested with XbaI, DraI, and SpeI followed by hybridization with rRNA and aac(6′)-Iz-specific probes indicated that the gene was located in the chromosome. Theaac(6′)-Iz gene was detected by DNA-DNA hybridization in all 80 strains of S. maltophilia tested. The MICs of gentamicin against these strains of S. maltophilia were lower than those of amikacin, netilmicin, and tobramycin, indicating that production of AAC(6′)-Iz contributes to aminoglycoside resistance in S. maltophilia.


2019 ◽  
Vol Volume 12 ◽  
pp. 511-519 ◽  
Author(s):  
Lijuan Xu ◽  
Ping Wang ◽  
Jing Cheng ◽  
Shangshang Qin ◽  
Weihong Xie

1998 ◽  
Vol 42 (1) ◽  
pp. 88-93 ◽  
Author(s):  
Gayatri Vedantam ◽  
Gordon G. Guay ◽  
Natasha E. Austria ◽  
Stella Z. Doktor ◽  
Brian P. Nichols

ABSTRACT A sulfathiazole-resistant dihydropteroate synthase (DHPS) present in two different laboratory strains of Escherichia colirepeatedly selected for sulfathiazole resistance was mapped tofolP by P1 transduction. The folP mutation in each of the strains was shown to be identical by nucleotide sequence analysis. A single C→T transition resulted in a Pro→Ser substitution at amino acid position 64. Replacement of the mutantfolP alleles with wild-type folP significantly reduced the level of resistance to sulfathiazole but did not abolish it, indicating the presence of an additional mutation(s) that contributes to sulfathiazole resistance in the two strains. Transfer of the mutant folP allele to a wild-type background resulted in a strain with only a low level of resistance to sulfathiazole, suggesting that the presence of the resistant DHPS was not in itself sufficient to account for the overall sulfathiazole resistance in these strains of E. coli. Additional characterization of an amplified secondary resistance determinant, sur, present in one of the strains, identified it as the previously identified bicyclomycin resistance determinant bcr, a member of a family of membrane-bound multidrug resistance antiporters. An additional mutation contributing to sulfathiazole resistance,sux, has also been identified and has been shown to affect the histidine response to adenine sensitivity displayed by thesepurU strains.


2008 ◽  
Vol 52 (8) ◽  
pp. 2929-2932 ◽  
Author(s):  
Vincent Cattoir ◽  
Patrice Nordmann ◽  
Jesus Silva-Sanchez ◽  
Paula Espinal ◽  
Laurent Poirel

ABSTRACT A novel QnrB-like plasmid-mediated resistance determinant, QnrB19, was identified from an Escherichia coli clinical isolate from Colombia. Its gene was associated with an ISEcp1-like insertion element that did not act as a promoter for its expression. Using an in vitro model of transposition, we showed that the ISEcp1-like element was able to mobilize the qnrB19 gene.


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