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PubMed1965

DRUG RESISTANCE OF STAPHYLOCOCCI. II. JOINT ELIMINATION AND JOINT TRANSDUCTION OF THE DETERMINANTS OF PENICILLINASE PRODUCTION AND RESISTANCE TO MACROLIDE ANTIBIOTICS.

Mitsuhashi, Susumu (Gunma University, Maebashi, Japan), Hajime Hashimoto, Megumi Kono, and Masato Morimura. Drug resistance of staphylococci. II. Joint elimination and joint transduction of the determinants of penicillinase production and resistance to macrolide antibiotics. J. Bacteriol. 89:988-992. 1965.-Strains of Staphylococcus aureus, which show high resistance to macrolide antibiotics (erythromycin, oleandomycin, leucomycin, and spiramycin) and the capacity to produce penicillinase, have been isolated from clinical sources. The determinants of penicillinase production (PCase(+)) and resistance to macrolide antibiotics (MAC(r)) of these strains were irreversibly eliminated by treatment with acridine or with ultraviolet light. Among the 18 strains tested, PCase(+) and MAC(r) were eliminated from all strains except one, which lost only PCase(+) but not MAC(r). The characters PCase(+) and MAC(r) were jointly transduced with the aid of phage lysates, obtained from the resistant donors by ultraviolet irradiation, into staphylococcal strains sensitive to PC and MAC. Segregation of PCase(+) and MAC(r) was rarely observed after transduction. From these results, it is suggested that the determinants of both PCase(+) and MAC(r) of staphylococci are located close together on a single genetic element, i.e., a plasmid (or episome), which exists extrachromosomally.

Anti-Bacterial Agents↗
PubMed1986

Induction of mutants resistant to antibiotics in Brevibacterium flavum.

The optimum conditions for the induction of mutants resistant to antibiotics in Brevibacterium flavum ATCC 14067 were determined. UV irradiation at the energy fluence of 6.5 kJ/m2 and N-methyl-N'-nitro-N-nitrosoguanidine (1 mg/mL) at pH 6.0 were used for the induction of mutants. Mutant strains resistant to rifampicin, oleandomycin, streptomycin and erythromycin were prepared.

Anti-Bacterial Agents↗
PubMed1986

Synergy of four macrolide antibiotics with chloroquine against chloroquine-resistant Plasmodium falciparum in vitro.

The antimalarial activity of four macrolide antibiotics was investigated against the multidrug resistant K1 strain of Plasmodium falciparum in vitro. ID50 (50% inhibitory concentration) values for erythromycin, spiramycin, tylosin tartrate and oleandomycin phosphate in 48-hour assays were 1.6 X 10(-4)M, 2.5 X 10(-5)M, 1.2 X 10(-5)M and 9 X 10(-6)M respectively, and in 96 hour assays were 10(-5)M, 2.6 X 10(-6)M, 2.6 X 10(-6) and 3 X 10(-6)M, respectively. Comparable values were obtained in assays in which drug effect was quantified from either parasite counts or 14C isoleucine incorporation. Each of the four macrolides displayed synergy with chloroquine at the IC90 (90% inhibitory concentration) level, but at the IC50 level synergy was either less pronounced or absent. For each combination this difference in the degree of synergy was significant at the 95% level of confidence. In replicate assays in which 3H hypoxanthine was the marker of drug effect, synergy between chloroquine and either erythromycin or spiramycin could not be detected.

Animals↗
PubMed1980

Mutagenicity of antibiotics in microbial assays. Problems of evaluation.

5 antibiotics, 4 of which inhibit protein synthesis in different ways, and 1 of which inhibits bacterial cell-wall synthesis, were tested in a battery of microbial assays for possible genetic effects. All the antibiotics, chloramphenicol, tetracycline, gentamicin, oleandomycin and phosphonomycin induced forward mutation to L-azetidine-2-carboxylic acid resistance in Escherichia coli WP2. This response was closely correlated with the toxic effects and was inferred to be deletion mutation. In addition, chloramphenicol was weakly active in reversion of the frame-shift mutation in Salmonella typhimurium TA98, gentamicin caused petite induction in S. cerevisiae at pH 4.4--4.7 and tetracycline gave a significant reponse with gene conversion and petite induction also in S. cerevisiae but at pH 7.2. The results, particularly those with E. coli, cast doubts on the validity of testing specifically designed antibacterial agents in bacteria, and raise serious problems in the evaluation of such data in terms to human populations.

Animals↗
PubMed1987

Determination of erythromycin in human plasma, using column liquid chromatography with a polymeric packing material, alkaline mobile phase and amperometric detection.

A method based on column liquid chromatography was developed for determination of plasma concentrations of erythromycin. PRP-1, a polymeric type of packing material suitable for chromatography and amperometric detection at high pH, was used. The effect of pH on the column performance and on the electrochemical response was studied. A pH of ca. 10 was found to be optimal. After extraction with tert.-butyl methyl ether, plasma concentrations down to 0.2 mumol/l could be measured, using automated sample injection. Oleandomycin was used as internal standard. The method was used for determination of plasma concentrations in a pharmacokinetic study under steady-state conditions.

Chromatography, Liquid↗
PubMed1995

Determination of erythromycin in gastric juice and blood plasma by liquid chromatography and electrochemical detection.

A liquid chromatographic method for determination of the antibiotic erythromycin in biological samples is described. Erythromycin and the internal standard, oleandomycin, were extracted from alkalinized samples with a mixture of 1-hexane and 2-butanol. After evaporation and reconstitution of the sample, separation was performed on a base-deactivated octadecylsilica column. The effects of pH in the mobile phase and of column temperature on the chromatographic performance were studied. Multiple and irregularly shaped peaks were obtained for some chromatographic systems, but by choosing appropriate conditions erythromycin could be eluted as a single symmetric peak. The absolute recovery was above 90% for erythromycin from blood plasma and above 85% from gastric juice. The limits of quantitation were 20 nM and 100 nM, respectively. Comparison of analytical results for a series of authentic samples with a microbiological assay showed excellent agreement.

Biological Assay↗
PubMed1993

Simple methods for the qualitative identification and quantitative determination of macrolide antibiotics.

Pyrolysis-gas chromatography is shown to be a rapid straightforward method for the qualitative differentiation of the macrolide antibiotics erythromycin, oleandomycin, troleandomycin, spiramycin and tylosin. Organic salts do not interfere and identification of erythromycin and troleandomycin in commercial products is viable. Spectrophotometric quantitation of these same five antibiotics after reaction with concentrated sulphuric acid is studied at about 470 nm. Reaction conditions such as acid concentration, time and temperature are provided. The sugar moieties of the antibiotics are proposed as the reactive sites. Detection limits are about 0.2-1.0 microg ml-1 [corrected] and analysis of pharmaceutical products should be possible.

Anti-Bacterial Agents↗
PubMed1990

Determination of erythromycin base and 2'-acetylerythromycin in human plasma using high-performance liquid chromatography with electrochemical detection.

A high-performance liquid chromatographic method for the determination of plasma concentrations of erythromycin base and 2'-acetylerythromycin, an ester prodrug of erythromycin, is described. tert.-Butyl methyl ether extracts of 1-ml plasma samples (pH 10) were chromatographed on a C18 reversed-phase column. A three-electrode coulometric detector (oxidation potentials +0.65 and +0.85 V) was used for quantitation. Oleandomycin was used as an internal standard. The method has good precision and accuracy, is linear in the range 0.25-7.5 mg/l and has proved to be suitable for pharmacokinetic studies in humans. Correlation with a microbiological assay was satisfactory (r greater than or equal to 0.95), but the chromatographic method gave ca. 30% higher values.

Biological Availability↗
PubMed2005

Probing the breadth of macrolide glycosyltransferases: in vitro remodeling of a polyketide antibiotic creates active bacterial uptake and enhances potency.

The glycan portion of macrolide antibiotics modulates their efficacy. High-level expression of three macrolide GTs and kinetic analysis has revealed a highly selective synthetic "tool kit" with such plasticity that 12 glycan-modified macrolide antibiotics have been readily created. One of these (1-Gal) is enhanced over its parent oleandomycin (1) by "glycotargeting", allowing higher uptake through active internalization by virtue of the attachment of a glycan (Gal) not normally found on 1. Subsequent release of the targeting glycan by endogenous galactosidase activity releases 1.

Anti-Bacterial Agents↗
PubMed2004

Determination of five macrolide antibiotic residues in honey by LC-ESI-MS and LC-ESI-MS/MS.

Liquid chromatography-electrospray ionization mass spectrometry methods (LC-ESI-MS and LC-ESI-MS/MS) for the determination of five macrolide antibiotics including spiramycin, tilmicosin, oleandomycin, erythromycin, and tylosin in honey are presented. Macrolides were protonated to form singly and/or doubly charged pseudomolecular ions, depending on their chemical structures, in an electrospray positive ionization mode. Data acquisition under MS/MS was achieved by applying multiple reaction monitoring (MRM) of two or three fragment ion transitions to provide a high degree of sensitivity and specificity. The recoveries, that is, determined by LC-ESI-MS/MS, of the five macrolides at fortified levels of 6, 16, 40, and 80 microg/kg ranged from 75.5 to 135.7% in light honey and from 42.1 to 111.0% in dark honey. The ion ratios obtained under MS/MS were key criteria to confirm the identity of macrolides in incurred samples. LC-ESI-MS/MS method detection limits of the five macrolides were <0.1 microg/kg.

Anti-Bacterial Agents↗
PubMed2002

Engineering specificity of starter unit selection by the erythromycin-producing polyketide synthase.

Chain initiation on many modular polyketide synthases is mediated by acyl transfer from the CoA ester of a dicarboxylic acid, followed by decarboxylation in situ by KSQ, a ketosynthase-like decarboxylase domain. Consistent with this, the acyltransferase (AT) domains of all KSQ-containing loading modules are shown here to contain a key arginine residue at their active site. Site-specific replacement of this arginine residue in the oleandomycin (ole) loading AT domain effectively abolished AT activity, consistent with its importance for catalysis. Substitution of the ole PKS loading module, or of the tylosin PKS loading module, for the erythromycin (ery) loading module gave polyketide products almost wholly either acetate derived or propionate derived, respectively, instead of the mixture found normally. An authentic extension module AT domain, rap AT2 from the rapamycin PKS, functioned appropriately when engineered in the place of the ole loading AT domain, and gave rise to substantial amounts of C13-methylerythromycins, as predicted. The role of direct acylation of the ketosynthase domain of ex-tension module 1 in chain initiation was confirmed by demonstrating that a mutant of the triketide synthase DEBS1-TE, in which the 4'-phosphopante-theine attachment site for starter acyl groups was specifically removed, produced triketide lactone pro-ducts in detectable amounts.

Acyltransferases↗
PubMed2000

Glycosylation of macrolide antibiotics. Purification and kinetic studies of a macrolide glycosyltransferase from Streptomyces antibioticus.

The oleD gene has been identified in the oleandomycin producer Streptomyces antibioticus and it codes a macrolide glycosyltransferase that is able to transfer a glucose moiety from UDP-glucose (UDP-Glc) to many macrolides. The glycosyltransferase coded by the oleD gene has been purified 371-fold from a Streptomyces lividans clone expressing this protein. The reaction product was isolated, and its structure determined by NMR spectroscopy. The kinetic mechanism of the reaction was analyzed using the macrolide antibiotic lankamycin (LK) as substrate. The reaction operates via a compulsory order mechanism. This has been shown by steady-state kinetic studies and by isotopic exchange reactions at equilibrium. LK binds first to the enzyme, followed by UDP-glucose. A ternary complex is thus formed prior to transfer of glucose. UDP is then released, followed by the glycosylated lankamycin (GS-LK). A pH study of the reaction was performed to determine values for the molecular pK values, suggesting possible amino acid residues involved in the catalytic process.

Amino Acid Sequence↗
PubMed1989

Comparison of the in-vitro effect of several macrolides on the oxidative burst of human neutrophils.

We have compared the in-vitro interaction of five macrolides (roxithromycin, erythromycin, spiramycin, oleandomycin and josamycin) with human neutrophils (PMN). Only roxithromycin strongly impaired the oxidative burst of PMN assessed by luminol amplified chemiluminescence, superoxide anion generation, and myeloperoxidase-mediated iodination of proteins. This effect was observed only for high concentrations of this drug (100 and 50 mg/l). Furthermore, the sensitivity of PMN to the depressive effect of roxithromycin permitted the definition of two kinds of PMN: in Highly Sensitive (HS)-PMN, the oxidative response was completely abolished while in Moderately Sensitive (MS)-PMN, a decreased, but yet measurable (20-50% of the control), response was obtained. The roxithromycin-induced depression of PMN was time-dependent and partly reversed by washing. Chemotaxis was also impaired by roxithromycin (100 mg/l) but phagocytosis of Klebsiella pneumoniae was unaltered even at high concentrations of the drug. Since roxithromycin displays the highest intracellular uptake, compared with the other macrolides assessed in this study, this could explain the results observed here. The relevance to the clinical situation needs further study. This effect of roxithromycin could be useful to control the inflammatory process associated in certain infectious diseases, in particular if high concentrations of the drug are obtained in tissues.

Anti-Bacterial Agents↗
PubMed2001

Characterization of the mac-1 gene encoding a putative ABC transporter from Myxococcus xanthus.

The mac-1 gene of Myxococcus xanthus TA, an antibiotic TA producer, encoded a protein with strong sequence similarity to the antibiotic ATP-binding cassette (ABC) transporter for macrolide antibiotics. The mac-1 gene encoding protein (Mac-1) had two ATP-binding domains containing Walker A and B motifs, and no hydrophobic transmembrane regions. Insertional inactivation of mac-1 caused enhanced sensitivity to oleandomycin, a macrolide antibiotic, while the mac-1 mutant showed normal export of antibiotic TA into the extracellular fluid. The mac-1 mutant could form mounds, but was unable to form fruiting bodies or sporulate under nutrient starvation. A primary role for Mac-1 in M. xanthus may be as a transporter which exports or imports a molecule required for the sporulation process.

ATP-Binding Cassette Transporters↗
PubMed1997

A dyadic plasmid that shows MLS and PMS resistance in Staphylococcus aureus.

Out of a collection of 56 Staphylococcus aureus clinical strains from 1971 to 1990 in Japan, we found one 1971 isolate, strain MS8968, harboring plasmid pMS97. A transductant strain, MS15009(pMS97), showed inducible resistance to a group of drugs, the so-called MLS antibiotics in the presence of a low concentration of erythromycin (EM). However, in the case of oleandomycin (OL), the strain showed resistance to another group of antibiotics: 14-membered macrolides (EM and OL), a 16-membered macrolide (mycinamicin I), and type B streptogramin, the so-called PMS antibiotics. Moreover, plasmid pMS97 contained an erm gene with universal primers specific for erm A, AM, B, BC, C, C', and G and an msrA gene with primers specific for msrA. The first finding suggests that two genes encoding functionally different mechanisms for MLS and PMS resistance, erm and msrA, are present together within plasmid pMS97 originating from S. aureus.

Anti-Bacterial Agents↗
PubMed2002

Purification and characterization of an erythromycin esterase from an erythromycin-resistant Pseudomonas sp.

An erythromycin esterase (molecular mass 51200 Da) was purified from Pseudomonas sp. GD100, which was isolated from a salmon hatchery sediment sample from Washington State. The pI of the protein was 4.5-4.8. The enzyme was inhibited by 1 mM mercuric acid, and had the substrate specificity for structurally related 14-membered macrolides, which decreased in the order of oleandomycin, erythromycin A and erythromycin A enol ether. The activity for erythromycin A varied with temperature, but the effect of pH was minimal at pH 6.0-9.0. The half-life of the enzyme was estimated to be 8.9 h at 35 degrees C and 0.23 h at 55 degrees C, and the activation energy of the catalytic reaction of erythromycin A was estimated at 16.2 kJ mol(-1).

Carboxylic Ester Hydrolases↗
PubMed1976

Effect of antibiotics and chemotherapeutics on the cytotoxic reaction between HL-A antigens and corresponding sera.

Effects of antibiotics and chemotherapeutics on the interaction between the HL-A antigens and the corresponding lymphocytotoxic sera vary from case to case. Streptomycin, oleandomycin, cephaloridine and kanamycin completely inhibit the cytotoxic reaction when added in the first or second stage of the test. Cytembena weakens the reaction while chlortetracyclin exhibits various effects. The rest of the drugs under investigation proved ineffective.

Anti-Bacterial Agents↗
PubMed1986

Contribution of two different mechanisms to erythromycin resistance in Escherichia coli.

Escherichia coli BM2570 was resistant to high levels of erythromycin by two different mechanisms. The two genes conferring resistance to erythromycin in BM2570 were carried by a 150-kilobase self-transferable plasmid, pIP1527, and were cloned separately in E. coli. A single polypeptide with an Mr of 27,000 was encoded by the gene erxA and conferred high-level resistance to macrolide, lincosamide, and streptogramin B-type antibiotics by a mechanism other than drug inactivation. This resistance phenotype, not previously reported for a clinical isolate of enterobacteria, was probably due to modification of the ribosomes. The gene ereB encoded an enzyme with an Mr of 51,000 which inactivated erythromycin and oleandomycin. The two different mechanisms specified by erxA and ereB contributed in more than an additive fashion to the high level of resistance to erythromycin conferred by plasmid pIP1527 to E. coli BM2570.

Bacterial Proteins↗