scholarly journals Relationship between Spontaneous Aminoglycoside Resistance in Escherichia coli and a Decrease in Oligopeptide Binding Protein

1998 ◽  
Vol 180 (20) ◽  
pp. 5484-5488 ◽  
Author(s):  
Keiko Kashiwagi ◽  
Maria Heloisa Tsuhako ◽  
Kaori Sakata ◽  
Tomoko Saisho ◽  
Atsuko Igarashi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Amino Acid Position ◽  
Aminoglycoside Antibiotics ◽  
Wild Type ◽  
Aminoglycoside Resistance ◽  
Resistant Mutants ◽  
Oligopeptide Transport System ◽  
Translational Level ◽  
Cells Cultured

ABSTRACT Changes in the amount of oligopeptide binding protein (OppA) in spontaneous kanamycin-resistant mutants of Escherichia coliwere investigated. Among 20 colonies obtained from 108cells cultured in the presence of 20 μg of kanamycin/ml, 1 colony had no detectable OppA and 7 colonies were mutants with reduced amounts of OppA. Sensitivity of wild-type cells to kanamycin increased slightly by transformation of the oppA gene, but the sensitivity of the mutants increased greatly by the transformation. A mutant with no OppA was found to be a nonsense mutant of the oppA gene at amino acid position 166. In a mutant having a reduced level of OppA, the reduction was due to the decrease in OppA synthesis at the translational level. These mutants were also resistant to other aminoglycoside antibiotics, including streptomycin, neomycin, and isepamicin. Isepamicin uptake activities decreased greatly in these two kinds of mutants. The results support the proposition that aminoglycoside antibiotics are transported into cells by the oligopeptide transport system, and that transport is an important factor for spontaneous resistance to aminoglycoside antibiotics.

scholarly journals OppA Escherichia coli mutants have osmodependent resistance to aminoglycoside antibiotics

1998 ◽  
Vol 21 (1) ◽  
pp. 15-19 ◽  
Author(s):  
Maria H. Tsuhako ◽  
Luis Carlos S. Ferreira ◽  
Sérgio Olavo P. da Costa
Keyword(s):  
Escherichia Coli ◽  
Cell Envelope ◽  
Growth Behavior ◽  
Aminoglycoside Antibiotics ◽  
Aminoglycoside Resistance ◽  
E Coli ◽  
Resistant Mutants ◽  
Oligopeptide Permease

The oligopeptide permease (OppA) protein was found to be missing in the periplasmic fractions of Escherichia coli kanamycin-resistant mutants selected under high osmotic conditions. The growth behavior of one mutant in media containing kanamycin or the toxic peptide triornithine suggests that OppA and another cell envelope component contribute to the osmolarity-dependent aminoglycoside resistance of E. Coli.

scholarly journals Resistance of Streptococcus pneumoniaeto Deformylase Inhibitors Is Due to Mutations indefB

2001 ◽  
Vol 45 (9) ◽  
pp. 2432-2435 ◽  
Author(s):  
Peter Margolis ◽  
Corinne Hackbarth ◽  
Sara Lopez ◽  
Mita Maniar ◽  
Wen Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Streptococcus Pneumoniae ◽  
Peptide Deformylase ◽  
Wild Type ◽  
Resistance Phenotype ◽  
Resistant Mutants

ABSTRACT Resistance to peptide deformylase inhibitors in Escherichia coli or Staphylococcus aureus is due to inactivation of transformylase activity. Knockout experiments in Streptococcus pneumoniae R6x indicate that the transformylase (fmt) and deformylase (defB) genes are essential and that adef paralog (defA) is not. Actinonin-resistant mutants of S. pneumoniae ATCC 49619 harbor mutations indefB but not in fmt. Reintroduction of the mutated defB gene into wild-type S. pneumoniaeR6x recreates the resistance phenotype. The altered enzyme displays decreased sensitivity to actinonin.

scholarly journals Characterization of Mutations Contributing to Sulfathiazole Resistance in Escherichia coli

1998 ◽  
Vol 42 (1) ◽  
pp. 88-93 ◽  
Author(s):  
Gayatri Vedantam ◽  
Gordon G. Guay ◽  
Natasha E. Austria ◽  
Stella Z. Doktor ◽  
Brian P. Nichols
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Position ◽  
Resistance Determinant ◽  
Nucleotide Sequence Analysis ◽  
Wild Type ◽  
Secondary Resistance ◽  
E Coli ◽  
Additional Mutation ◽  
Membrane Bound

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.

scholarly journals Increase of sensitivity to aminoglycoside antibiotics by polyamine-induced protein (oligopeptide-binding protein) in Escherichia coli.

1992 ◽  
Vol 174 (13) ◽  
pp. 4331-4337 ◽  
Author(s):  
K Kashiwagi ◽  
A Miyaji ◽  
S Ikeda ◽  
T Tobe ◽  
C Sasakawa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Aminoglycoside Antibiotics

scholarly journals The Periplasmic Protein MppA Requires an Additional Mutated Locus To Repress marA Expression in Escherichia coli

2003 ◽  
Vol 185 (4) ◽  
pp. 1465-1469 ◽  
Author(s):  
Xiaowen Bina ◽  
Vincent Perreten ◽  
Stuart B. Levy
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Antibiotic Susceptibility ◽  
Type Strain ◽  
Wild Type Strain ◽  
Binding Protein ◽  
Periplasmic Protein ◽  
Multiple Antibiotic Resistance ◽  
Wild Type ◽  
Expression In Escherichia Coli

ABSTRACT Escherichia coli strain TP985, which has an insertional mutation in the gene for the periplasmic murein tripeptide binding protein MppA, was previously reported to overproduce MarA and exhibit a multiple-antibiotic resistance (Mar) phenotype (H. Li and J. T. Park, J. Bacteriol. 181:4842-4847, 1999). We found that TP985 contained a previously unrecognized marR mutation which was responsible for the Mar phenotype. Transduction of the mppA mutation from TP985 to another wild-type strain did not affect antibiotic susceptibility. Overproduction of MppA repressed marA transcription in TP985 but not in other mppA or marR mutants. Therefore, TP985 contains an additional unknown mutation(s) that facilitates the repression of marA expression by MppA.

Isolation and characterization of catabolite repression-resistant mutants of Escherichia coli

1977 ◽  
Vol 23 (10) ◽  
pp. 1384-1393 ◽  
Author(s):  
Glen D. Armstrong ◽  
Hiroshi Yamazaki
Keyword(s):  
Escherichia Coli ◽  
Catabolite Repression ◽  
Coli Strain ◽  
Wild Type ◽  
Phosphotransferase System ◽  
E Coli ◽  
Isolation And Characterization ◽  
In The Wild ◽  
Resistant Mutants

A method has been developed for the isolation of Escherichia coli mutants which are resistant to catabolite repression. The method is based on the fact that a mixture of glucose and gluconate inhibits the development of chemotactic motility in the wild type, but not in the mutants. A motile E. coli strain was mutagenized and grown in glucose and gluconate. Mutants which were able to swim into a tube containing a chemotactic attractant (aspartic acid) were isolated. Most of these mutants were able to produce β-galactosidase in the presence of glucose and gluconate and were normal in their ability to degrade adenosine 3′,5′-cyclic monophosphate. Some of these mutants were defective in the glucose phosphotransferase system.

scholarly journals Altered expression of oligopeptide-binding protein (OppA) and aminoglycoside resistance in laboratory and clinical Escherichia coli strains

2000 ◽  
Vol 49 (5) ◽  
pp. 409-413 ◽  
Author(s):  
M.B. R. ACOSTA ◽  
R.C. C. FERREIRA ◽  
G. PADILLA ◽  
L.C. S. FERREIRA ◽  
S.O. P. COSTA
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Aminoglycoside Resistance ◽  
Altered Expression

scholarly journals Further studies on rod A mutant: A round morphological mutant of Escherichia coli K-12 with wild-type penicillin-binding protein 2.

1980 ◽  
Vol 44 (12) ◽  
pp. 2937-2941 ◽  
Author(s):  
Hiroshi MATSUZAWA ◽  
Sadamitsu ASOH ◽  
Takahisa OHTA ◽  
Shigeo TAMAKI ◽  
Michio MATSUHASHI
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Morphological Mutant ◽  
K 12
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