Isolation and Characterization of Tetracycline Resistance Proteins from
            <i>Staphylococcus aureus</i>
            and
            <i>Escherichia coli</i>

Wojdani, Aristo; Avtalion, Ramy R.; Sompolinsky, D

doi:10.1128/aac.9.3.526

Cited by 12 publications

(9 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A tetracycline-inducible inner membrane protein of molecular weight about 37,000, TET, is associated with TnlO-encoded resistance (8, 12), and a repressor activity of TET synthesis has been found (13). A TET protein of similar size encoded by other plasmid-borne resistance determinants has been described (8,12,(14)(15)(16).…”

mentioning

confidence: 99%

Active efflux of tetracycline encoded by four genetically different tetracycline resistance determinants in Escherichia coli.

McMurry¹,

Petrucci²,

Levy³

1980

Proc. Natl. Acad. Sci. U.S.A.

541

362

View full text Add to dashboard Cite

Tetracycline resistance encoded by four genetically different determinants residing on plasmids in Escherichia coli was shown to be associated in each case with an energy-dependent decrease in accumulation of the antibiotic in whole cells in which resistance had been induced. The different class determinants examined were those on plasmids RP1 (class A), R222 (class B), R144 (class C), and RAI (class D). This decrease in accumulation was attributable to an active efflux, because everted (inside-out) membrane vesicles made from tetracycline-induced E. coli cells containing any one of the four plasmids were shown to concentrate tetracycline by an active influx. This active uptake was not seen in inside-out vesicles from sensitive cells or uninduced R222-containing cells. In vesicles from induced R222-containing cells, the efflux appeared to be carrier-mediated with a Km of about 6 ;M. These results demonstrate that active export of tetracycline is a common component of the mechanism for tetracycline resistance encoded by different plasmid-borne determinants in bacteria. The tetracyclines are bacteriostatic antibiotics used to treat a broad spectrum of microbial disease agents in humans, animals, and plants (1). They act by inhibiting protein synthesis, specifically by preventing aminoacyl tRNA from binding to the A site on the ribosome during peptide elongation (2-4). Bacterial resistance to tetracycline is widespread and is caused by at least four different resistance determinants (5) carried on plasmids in the host bacterial cell. In most cases, resistance is inducible by subinhibitory amounts of tetracycline, and for some plasmids it can reach 200 times the resistance of plasmidless cells. The most common tetracycline resistance determinant in Escherichia coli appears to be that borne on transposon TnlO.t Plasmid-mediated tetracycline resistance does not lead to inactivation of the tetracycline molecule (6-8). Rather, resistance is associated with a decrease in tetracycline accumulation (8-11). A tetracycline-inducible inner membrane protein of molecular weight about 37,000, TET, is associated with TnlO-encoded resistance (8, 12), and a repressor activity of TET synthesis has been found (13). A TET protein of similar size encoded by other plasmid-borne resistance determinants has been described (8,12,(14)(15)(16).In previous work we showed two transport systems for tetracycline in sensitive E. coli K-12 cells, only one of which was sensitive to energy inhibitors (17). Both were altered by the tetracycline resistance plasmid R222 (11). The energy-dependent component of uptake in sensitive cells was replaced in resistant cells by a non-energy-requiring uptake of a lesser rate. In addition, the energy-independent uptake system in sensitive cells was decreased to 1/3-1/5 (11). This decrease appeared to be at least partly reversed by energy inhibitors (11), which suggested that energy was required for the lowered tetracycline accumulation. Using everted membrane vesicles, we now demonstrate that resistant...

show abstract

mentioning

confidence: 99%

Active efflux of tetracycline encoded by four genetically different tetracycline resistance determinants in Escherichia coli.

McMurry¹,

Petrucci²,

Levy³

1980

Proc. Natl. Acad. Sci. U.S.A.

541

362

View full text Add to dashboard Cite

show abstract

“…Media and solutions used as well as the way of harvesting of bacteria were as described [1]. The bacteria were suspended in a solution of 0.05 M tris (hydroxymethyl)-amino-methane (Tris)-HC1, 0.145 M NaC1, 0.045 M magnesium acetate, 10/~g/ml DNAase and 50 gg/ml lysostaphin at pH 7.5 until the turbidity was reduced to 20% or less.…”

Section: Growth Conditions and Preparative Methodsmentioning

confidence: 99%

“…The samples were hydrolyzed and examined with a Technicon System amino acid auto analyzer as described [ 1 ]. Tryptophan was determined separately after oxidation with N-bromosuccinimide [5] and cystine-cysteine were determined as cysteic acid after oxidation with performic acid [6].…”

Section: Amino Acid Analysis Of Teramentioning

confidence: 99%

“…In a previous report [ 1 ] we described the isolation and purification of an antigenic protein 'from cell wails of Staphylococcus aureus 111, which contains a tetracycline (Tc) plasmid ; this protein could not be demonstrated in 111 after elimination of the Tc plasmid (111-elim). By disk electrophoresis in SDS-polyacrylamide the molecular weight was estimated as 32 000 and a preliminary amino acid analysis was reported.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Tetracycline resistance antigen fromStaphylococcus aureus

Sompolinsky¹,

Hammerman²,

O³

et al. 1978

FEMS Microbiology Letters

View full text Add to dashboard Cite

“…The induction of tetracycline resistance by sublethal concentrations of the antibiotic can be prevented by inhibitors of ribonucleic acid or protein synthesis (10). Resistant cells contain a protein not found in sensitive strains (14)(15)(16), and this protein can be released from Escherichia coli by osmotic shock (4). D-Cycloserine is an analogue of D-alanine and is therefore an inhibitor of DL-alanine racemase (EC 5.1.1.1) (6) and n-alanine:n-alanine ligase (EC 6.3.2.4) (8).…”

mentioning

confidence: 99%

Inducible Resistance to d -Cycloserine in Bacillus subtilis 168

Clark

Young

1977

Antimicrob Agents Chemother

View full text Add to dashboard Cite

Resistance to D-cycloserine could be induced in Bacillus subtilis 168 by sublethal concentrations of D-cycloserine. Sensitivity to the antibiotic could be regained by growth in the absence of D-cycloserine. The bactericidal activity of )-cycloserine apparently was not altered by resistant cells, and peptidoglycan synthesis was still inhibited by D-cycloserine in resistant cells. The n-cycloserine resistance apparently resulted from a decreased uptake of the antibiotic. The decrease in n-cycloserine transport could be prevented by simultaneous treatment of the cells with rifampin and n-cycloserine. r.-Cycloserine was transported by the same system as glycine in B. subtilis. D-Cycloserine was able to exchange for intracellular glycine in both sensitive and resistant cells, suggesting that Dcycloserine is not excluded from the cell in resistant cultures.

show abstract

Isolation and Characterization of Tetracycline Resistance Proteins from Staphylococcus aureus and Escherichia coli

Cited by 12 publications

References 15 publications

Active efflux of tetracycline encoded by four genetically different tetracycline resistance determinants in Escherichia coli.

Active efflux of tetracycline encoded by four genetically different tetracycline resistance determinants in Escherichia coli.

Tetracycline resistance antigen fromStaphylococcus aureus

Inducible Resistance to d -Cycloserine in Bacillus subtilis 168

Contact Info

Product

Resources

About