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At least 217 records · Page 12Linked to original sources

Absorption of lincomycin through the respiratory pathways and its influence on alveolar macrophages after aerosol administration to chickens.

A concentration of 250 mg m-3 lincomycin was administered by aerosol to 40 chickens, weighing between 1900 and 2200 g. The birds were killed in groups of five at different intervals after dosing, and the trachea, lungs and blood serum were examined for antibiotic content by bioassay. The antibiotic was present at high levels in the trachea for one to 24 hours, and significant levels were present in the lungs and serum. Respiratory macrophages were obtained from the lungs and air sacs of the chickens by lavaging through the surgically prepared trachea with a paediatric urinary catheter. The macrophages were identified by morphology as round or slightly amorphous, refractile, frequently grannular cells; they phagocytosed Staphylococcus aureus 6538.

Aerosols↗

Lincomycin treatment of guinea pigs causes formation of pigmented phosphate containing gallbladder sludge and stones.

We studied the mechanism of gallbladder sludge formation in guinea pigs (n = 30) treated with lincomycin (80 mg/kg/day) for 7 consecutive days. At sacrifice (day 8) gallbladders of treated animals contained turbid bile, sludge and in one animal a single gallstone. The precipitates were amorphous on X-ray diffraction. Infra-red spectroscopy revealed calcium phosphate as the major component. Compared to saline-treated controls (n = 15) concentrations of total protein, total phosphate and total bilirubin in gallbladder bile were significantly increased (P less than 0.05). The increase in total phosphate was due to the inorganic component, since phospholipid phosphorus was unchanged. The relative amounts of unconjugated bilirubin and of bilirubin mono- and diconjugates in gallbladder bile were unaffected by treatment as was beta-glucuronidase activity. However, sludge was enriched in unconjugated bilirubin compared to gallbladder bile. This was most probably caused by alkaline hydrolysis of bilirubin monoconjugates. To some extent, disproportionation of bilirubin monoconjugates in bile or sludge, either in vivo or during sample preparation, might also have led to increased unconjugated pigment.

Animals↗

Failure of antibiotics gentamycin, tylosin, lincomycin and spectinomycin to eliminate Mycoplasma bovis in artificially infected frozen bovine semen.

To study the effect of antibiotics upon Mycoplasma bovis in fresh bovine semen just before freezing, specimens of bovine semen were artificially infected with 1 of 9 different strains of M. bovis. Inocula of each strain were prepared to contain 10(5) to 10(6)/mL colony-forming units of M. bovis at 3 different stages of the growth phase. The infected semen was diluted with a Tris extender by a 3-step procedure using an antibiotic mixture of gentamicin, tylosin, lincomycin and spectinomycin (GTLS). This semen-antibiotic mixture was placed into French straws that were stored at -196 degrees C. The control semen specimens contained no antibiotics Mycoplasmas were counted after 8 d of storage in 3 decimal dilutions of the frozen semen. No evident effect was noticed upon the 9 tested strains of mycoplasmas in the semen frozen with the antibiotics, compared with that of the untreated control samples. It was further shown that this lack of effect was irrespective of the stage of the growth phase of the mycoplasmas. It was concluded that the antibiotic mixture (GTLS) in semen specimens is not capable of total elimination of mycoplasmas in frozen bovine semen.

Animals↗

Analysis of a formulation containing lincomycin and spectinomycin by liquid chromatography with pulsed electrochemical detection.

A reversed phase ion-pair liquid chromatographic method using a base deactivated column and pulsed electrochemical detection on a gold electrode is described. It allows the separation of a mixture of spectinomycin sulfate, lincomycin hydrochloride and their related substances. A step gradient was necessary to obtain a good separation together with a reasonable analysis time of 40 min. The mobile phases consisted of an aqueous solution of 3.3 or 0.55 g/l pentanesulfonic acid, 10 mM acetic acid and 20 ml/l tetrahydrofuran. Both mobile phases were adjusted to pH 4.0 with diluted sodium hydroxide. The influence of the different chromatographic parameters on the separation was investigated. Two commercial samples were analyzed using the described method. In total 12 components could be separated.

Anti-Bacterial Agents↗

Therapeutic efficacy of medicating drinking water with spectinomycin and lincomycin-spectinomycin in experimental Escherichia coli infection in poultry.

Although no microbiological activity was found in blood plasma during treatment of broilers through the drinking water with spectinomycin or lincomycin-spectinomycin, these drugs proved highly effective in treating experimentally induced colibacillosis. This efficacy may be produced by a metabolite or a degradation product of spectinomycin that reaches the infection site in the respiratory tract and interferes with adherence of bacteria.

Animals↗

Lincomycin resistance in methicillin-resistant Staphylococcus aureus strains of hospital origin.

A total of 170 Staphylococcus aureus strains isolated during a one-year period at the University Hospital of Patras Medical School were examined for resistance to a battery of antimicrobial agents by disk diffusion and minimum inhibitory concentration (MIC) determination. Fifty-five isolates were lincomycin- and methicillin-resistant (LMRSA). In the group of 55 LMRSA isolates 13 were also resistant to vancomycin. All the LMRSA isolates were not typed by the international set and the experimental phages 88A and 25 at routine typing dilution (RTD), while 18 isolates were lysed by phages at 100XRTD and 1000XRTD. Reverse phage-typing and heat shock treatment of the LMRSA isolates had no effect on their typability. Plasmid profiles coupled with restriction endonuclease analysis of plasmid DNA established that the LMRSA isolates represent different strains. Membrane-protein profiles by polyacrylamide gel electrophoresis (PAGE) showed that LMRSA strains could belong to one group. This method proved useful and sensitive for characterization of LMRSA.

Bacterial Proteins↗

A reliable two-hour Staphylococcus plate assay of rifampicin, erythromycin, lincomycin, chloramphenicol and amikacin in human sera.

A simple and precise agar diffusion microassay was developed for rifampicin (RIF) in serum. The method involved the addition of sera containing RIF (0.125-4.0 micrograms/ml) to wells cut in an agar medium (pH 6.6) surface seeded with an adjusted inoculum of Staphylococcus aureus ATCC 6538 P and incubated for 2h at 40 degrees C. Repetitive assays of sera containing known concentrations of RIF revealed an average mean recovery of 93.6% with a coefficient of variation of 5.7%. This rapid method allowed accurate determination of RIF in the presence of erythromycin, chloramphenicol, lincomycin and amikacin. These four antibiotics were also separately measured in sera by the rapid assay at different pH values.

Amikacin↗

Inducible or constitutive expression of resistance in clinical isolates of streptococci and enterococci cross-resistant to erythromycin and lincomycin.

Thirty-five of 40 clinical isolates of enterococci and streptococci cross-resistant to erythromycin and lincomycin and harbouring erm genes were inducibly resistant to these drugs, suggesting that ribosomal methylation is predominantly inducibly expressed in these bacterial genera. Regulatory regions located upstream of the erm genes of four inducible and three constitutive strains were amplified and sequenced. Expression of constitutive resistance in two strains of Streptococcus pneumoniae and Enterococcus faecalis could be accounted for by a large deletion or a DNA duplication within the regulatory regions, respectively.

Anti-Bacterial Agents↗

Lincomycin abrogates dexamethasone-enhanced melanogenesis in B16 melanoma cells.

The effects of lincosamide, and interference between the effects of glucocorticoid and lincosamide, on melanogenesis were determined in B16 melanoma cells. Cells were treated for 4 days with lincomycin (LM) and/or dexamethasone (DX) at equimolar concentrations ranging from 10(-9) M to 10(-5) M, or at various concentrations of DX with 10(-6) M LM. Effects on proliferation, tyrosinase activity, melanin biosynthesis, and levels of mRNA for tyrosinase, tyrosinase-related protein 1 (TRP1), and tyrosinase-related protein 2 (TRP2) were examined. Treatment with LM or LM + DX stimulated proliferation of melanoma cells with minimal cytotoxicity, while DX did not influence cell proliferation either alone or in combination with LM. Treatment with LM alone increased tyrosinase activity slightly and reduced melanin content in a dose-dependent manner. However, LM counteracted the pronounced increase in tyrosinase elicited by DX and also abrogated the dose-dependent increase in melanin content elicited by DX. Treatment with LM alone did not affect mRNA levels for tyrosinase, TRP1, or TRP2. Furthermore, LM abrogated the DX-induced up-regulation of mRNAs for tyrosinase and the down-regulation of TRP1 mRNA. These results suggest that LM inhibits melanogenesis post-transcriptionally and abrogates glucocorticoid-induced melanogenesis at the transcriptional level in B16 melanoma cells.

Animals↗

Serum and peritoneal fluid concentrations of clindamycin and lincomycin in the mouse.

Serum concentrations of drug were obtained at various times after intramuscular dosing of healthy mice with either clindamycin or lincomycin hydrochlorides. Washings from the peritoneal cavity were taken at the same time as the serum samples. Changes in drug concentration in the peritoneal fluid with time mimic those for the serum, but concentrations in peritoneal fluid are much greater than the corresponding serum concentrations. The total volume of peritoneal fluid was estimated to be 0.05 ml.

Animals↗

Characterization of a small plasmid determining resistance to erythromycin, lincomycin, and vernamycin Balpha in a strain of Streptococcus sanguis isolated from dental plaque.

A plasmid determining resistance to erythromycin (inducible), lincomycin, and vernamycin B(alpha) was isolated from a strain of Streptococcus sanguis isolated from dental plaque of a patient who had been on erythromycin therapy for an extended period of time. The plasmid, designated pAM77, had a molecular weight of 4.5 x 10(6) and was present to the extent of one to two copies per bacterial chromosome. The plasmid could transform S. sanguis strain Challis.

Anti-Bacterial Agents↗

Effect of novobiocin and its combination with tetracycline, chloramphenicol, erythromycin, and lincomycin on the microbial generation of Escherichia coli.

Inhibition of the steady-state generation of Escherichia coli by the bacteriostatic antibiotic novobiocin is linearly related to drug concentration in the range of 0 to 30 mug/ml. Increased cell sizes result because the drug inhibits cell division. The generation rate dependence on drug concentration depends on the nonionized fraction of novobiocin and is invariant with inoculum size or medium composition. However, the antibacterial activity of novobiocin decreases as the concentration of nutrients and Mg(2+) increases, although the inhibitory action of novobiocin on generation rate remains unchanged for concentrations of Mg(2+) above 8.1 x 10(-4) M. Novobiocin is synergistic in combinations with tetracycline in broth, but not when the Mg(2+) was maintained at 4.05 x 10(-3) M. Combinations of novobiocin with the 50S ribosomal subunit inhibitors chloramphenicol, erythromycin, or lincomycin are antagonistic, and the degree of growth inhibition is determined only by that component of the binary combination that would have the greater potency if it were acting alone.

Cell Division↗

Lincomycin resistance mutations in two regions immediately downstream of the -10 region of lmr promoter cause overexpression of a putative multidrug efflux pump in Bacillus subtilis mutants.

We isolated 19 lincomycin-resistant Bacillus subtilis mutants by expressing lmrB encoding a putative multidrug efflux protein. Eighteen of the mutants altered at two regions (-3 to -1 and +15) immediately downstream of the -10 region of the lmr promoter increased lmr transcription in vivo and in vitro.

Bacillus subtilis↗

In vitro development of resistance to erythromycin, other macrolide antibiotics, and lincomycin in Mycoplasma pneumoniae.

Mycoplasma pneumoniae was made highly resistant to erythromycin in vitro by serial subculture in broth media containing erythromycin. The resistance developed to erythromycin was 200 mug/ml with the Mac strain, a prototype of M. pneumoniae, and 10 mug/ml with the Fukumura strain, an isolate. The erythromycin resistance was accompanied by cross resistance to other macrolide antibiotics (leucomycin, josamycin, spiramycin, and oleandomycin) and to lincomycin, but there was no resistance to vernamycin B. Resistance to the antibiotics developed in vitro or in vivo was stable after the microorganisms were repeatedly transferred in antibiotic-free media.

Anti-Bacterial Agents↗

Transferability of macrolide, lincomycin, and streptogramin resistances between group A, B, and D streptococci, Streptococcus pneumoniae, and Staphylococcus aureus.

The transferability of plasmid pRI405 between various streptococci of groups A, B, and D, Streptococcus pneumoniae, and Staphylococcus aureus is described. pRI405 originated from Streptococcus faecalis and encodes for resistance to macrolides, lincomycin, and streptogramin B (MLS resistance). The host range of the well-documented streptococcal plasmid pAM beta 1 was found to be similar to that of pRI405. Cleavage with restriction enzymes suggests that pRI405 belongs to a related family of MLS resistance plasmids.

Anti-Bacterial Agents↗

Characterization of a Bacteroides mobilizable transposon, NBU2, which carries a functional lincomycin resistance gene.

The mobilizable Bacteroides element NBU2 (11 kbp) was found originally in two Bacteroides clinical isolates, Bacteroides fragilis ERL and B. thetaiotaomicron DOT. At first, NBU2 appeared to be very similar to another mobilizable Bacteroides element, NBU1, in a 2.5-kbp internal region, but further examination of the full DNA sequence of NBU2 now reveals that the region of near identity between NBU1 and NBU2 is limited to this small region and that, outside this region, there is little sequence similarity between the two elements. The integrase gene of NBU2, intN2, was located at one end of the element. This gene was necessary and sufficient for the integration of NBU2. The integrase of NBU2 has the conserved amino acids (R-H-R-Y) in the C-terminal end that are found in members of the lambda family of site-specific integrases. This was also the only region in which the NBU1 and NBU2 integrases shared any similarity (28% amino acid sequence identity and 49% sequence similarity). Integration of NBU2 was site specific in Bacteroides species. Integration occurred in two primary sites in B. thetaiotaomicron. Both of these sites were located in the 3' end of a serine-tRNA gene NBU2 also integrated in Escherichia coli, but integration was much less site specific than in B. thetaiotaomicron. Analysis of the sequence of NBU2 revealed two potential antibiotic resistance genes. The amino acid sequences of the putative proteins encoded by these genes had similarity to resistances found in gram-positive bacteria. Only one of these genes was expressed in B. thetaiotaomicron, the homolog of linA, a lincomycin resistance gene from Staphylococcus aureus. To determine how widespread elements related to NBU1 and NBU2 are in Bacteroides species, we screened 291 Bacteroides strains. Elements with some sequence similarity to NBU2 and NBU1 were widespread in Bacteroides strains, and the presence of linA(N) in Bacteroides strains was highly correlated with the presence of NBU2, suggesting that NBU2 has been responsible for the spread of this gene among Bacteroides strains. Our results suggest that the NBU-related elements form a large and heterogeneous family, whose members have similar integration mechanisms but have different target sites and differ in whether they carry resistance genes.

Amino Acid Sequence↗