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PubMed1996

Comparative killing kinetics of methicillin-resistant Staphylococcus aureus by bacitracin or mupirocin.

The in vitro activities of bacitracin and mupirocin were compared for seven different strains of methicillin-resistant Staphylococcus aureus. Six of seven strains showed bacitracin minimum inhibitory concentrations (MICs) of 0.5 to 1.0 units/mL, and all seven had mupirocin MICs of 0.5 to 2 micrograms/mL. Time-kill studies revealed 2.6- to 4.5-log reduction in 24 hours with strains susceptible to bacitracin (4 units/mL) and 0 to 2.2 reduction with mupirocin (16 micrograms/mL). Bacitracin should be considered further for in vivo studies because of enhanced bacteriocidal effect and lower cost.

Anti-Bacterial Agents↗
PubMed2000

Effect of zinc bacitracin and salinomycin on intestinal microflora and performance of broilers.

A feeding experiment was carried out over 42 d with four groups of broiler chickens fed experimental diets formulated to provide no supplementation, 20 mg zinc bacitracin, 60 mg salinomycin, or both feed additives in combination. During the fifth week of the experiment, four chickens from each pen were killed, and the contents of gizzard, duodenum, jejunum, ileum, ceca, and rectum were separately collected and pooled. In all intestinal segments, the pH and the concentration of lactic acid were measured, and the numbers of anaerobic bacteria, coliforms, lactic acid bacteria, lactobacilli, enterococci, and Clostridium perfringens were counted. In homogenates of pancreas obtained from four animals, the activities of amylase, lipase, trypsin, and chymotrypsin were measured. A significant growth-promoting effect was observed in the group receiving zinc bacitracin in combination with salinomycin. Zinc bacitracin significantly reduced the number of coliform bacteria in the ileum and increased the activities of amylase and lipase in pancreas homogenates. Supplementation with salinomycin and zinc bacitracin, alone or in combination, resulted in significantly lower counts of C. perfringens as well as Lactobacillus salivarius, which was a dominant lactic acid bacterium found in broiler intestinal contents. High numbers of these lactobacilli may play a role in broiler growth depression related to competition in nutrient uptake or impaired fat absorption due to bile acid deconjugation.

Amylases↗
PubMed1980

Regulation of bacitracin synthetase by divalent metal ions in Bacillus licheniformis.

The activity in vitro of the bacitracin synthetase of Bacillus licheniformis ATCC 10716 is influenced by divalent metal ions (Mg2+, Mn2+, Fe2+ or Co2+) and by bacitracin. It is possible that complexes between bacitracin and metal ions exert feedback control on the synthetase. An overall control mechanism for bacitracin synthetase may consist of substrate-metal ion complexes and product-metal ion complexes.

Amino Acids↗
PubMed1976

On the role of bacitracin peptides in trace metal transport by Bacillus licheniformis.

Bacitracin markedly increased the toxic effect of several divalent metal ions towards growth of the producer strain Bacillus licheniformis ATCCI4580. Magnesium ions antagonized the toxic effect of these divalent cations both in the presence and absence of bacitracin. It is suggested that bacitracin increases the uptake of several divalent metal ions. The function of the bacitracin peptides may be to extract essential divalent cations from 'waiting sites' on the surface of the cells and transfer the cations to the transport mechanisms in the cytoplasmic membrane.

Bacillus↗
PubMed1994

Antagonists of bacitracin.

Three groups of substances were identified which inhibit the bactericidal activity of bacitracin. Beside two divalent metals, Mg2+ and Ca2+, and a metabolite with chelating properties, citrate, the most pronounced effect was observed with pyrophosphate. Metals probably prevent access of bacitracin to the lipid carrier whereas metabolites with chelating properties deprive the bacitracin of a metal ion needed for its binding to the lipid carrier. Pyrophosphate, effective as an antagonist at very low concentrations, may intercept the binding of bacitracin to the pyrophosphate part of the target molecule.

Bacillus subtilis↗
PubMed1994

Bacitracin: a significant sensitizer in leg ulcer patients?

We report the results of patch testing 85 patients with either long-standing venous ulceration or eczema complicating their leg ulcers. As previously reported, lanolin and its derivatives and topical antibiotics were the most frequent sensitizers. However, unlike previously published data, we found bacitracin to be the most potent sensitizer of all topical antibiotics tested. There were no positive reactions in a control group of patients, although we were unable to repeat the patch tests in patients with a positive reaction to bacitracin. In the past 10 years, our department has used a proprietary mixture of polymyxin and bacitracin in treating infected leg ulcers and other dermatoses. It is therefore possible that chronic usage of topical bacitracin on leg ulcers carries a significant risk of contact sensitization.

Adult↗
PubMed1975

The effect of bacitracin and Mn(II)ions upon the producer strain Bacillus licheniformis.

The peptide antibiotic bacitracin is inhibitory to growth of the producer strain Bacillus licheniformis only in the presence of excess manganese(II)ions. Both the early and the late growth are inhibited in a similar manner upon addition of bacitracin and manganese(II)ions. Thus, B. licheniformis does not develop resistance to its own antibiotic during growth. Added bacitracin is stimulatory to growth of B. licheniformis in media with a very low content of manganese(II)ions. These results support the hypothesis that bacitracin participates in the manganese transport of the producer strain B. licheniformis.

Bacillus↗
PubMed1990

Bacitracin-induced proteins in Bacillus subtilis and Bacillus thuringiensis and their relationship with resistance.

Bacitracin induced one protein (bacitracin-induced protein [BIP]) in Bacillus thuringiensis and two proteins (BIP1 and BIP2) in Bacillus subtilis that were localized in the membrane. Divalent cations acted as cofactors for induction in all three cases. Growth was initially inhibited by the antibiotic, but following induction of proteins growth resumed. B. subtilis cells possessing BIPs were able to duplicate at a normal rate in the presence of bacitracin. The amount of B. subtilis BIPs diminished markedly after a few divisions in the absence of the antibiotic and the organism simultaneously reverted to the susceptible state. Induction of the proteins did not take place after the fourth or fifth hour of the stationary phase. The B. thuringiensis BIP was also induced by vancomycin. Bacitracin did not induce the synthesis of specific proteins in susceptible (Micrococcus lysodeikticus) or outer membrane-possessing resistant bacteria (Escherichia coli).

Bacillus subtilis↗
PubMed1977

In vitro production of bacitracin by proteolysis of vegetative Bacillus licheniformis cell protein.

The action of a sporulation-specific seryl protease on antibiotic-free extracts of Bacillus licheniformis cells yields a peptide that is identified as bacitracin by its biological activity, its spectral properties, and its comigration with genuine bacitracin in both paper and thin-layer chromatography. During proteolysis, a chemical structure is generated with the spectral properties of a delta-2 thiazoline ring. The yield in vitro, 4 microgram of bacitracin per mg of protein, is less than the maximal yield from sporulating cells, 75 microgram of bacitracin per mg of cell protein, but is a linear function of the amount of protein in the reaction system. Approximately 30% of the protein yielding the antibiotic is ribosomal associated, and only 25% of that amount can be removed by washing with 1 M NH4Cl. The substrate protein is a constant fraction of the cell protein throughout exponential growth and very early sporulation stages of culture development.

Bacillus↗
PubMed1981

Bacitracin and protease production in relation to sporulation during exponential growth of Bacillus licheniformis on poorly utilized carbon and nitrogen sources.

Growth of Bacillus licheniformis in a chemically defined medium containing glucose and ammonium chloride yielded a doubling time of 1.00 h. Examination of the culture during exponential growth revealed a lack of heat-resistant spores together with a complete absence of detectable concentrations of bacitracin or extracellular serine protease. Replacement of glucose as the sole carbon source by glycerol, pyruvic acid, citric acid, or lactic acid resulted in doubling times of 1.13, 2.00, 3.16, and 3.95 h, respectively. Bacitracin, protease, and heat-resistant spores were produced during exponential growth in amounts related to these doubling times. A qualitatively similar pattern was observed when ammonium chloride was replaced by sodium nitrate, alanine, or glutamic acid which gave doubling times of 1.65, 1.77, and 1.90 h, respectively. Protease, but not bacitracin, concentrations were substantially higher when the growth rate was restricted by use of poor nitrogen rather than poor carbon sources. The relationships between bacitracin production, protease production, and the sporulation process are discussed.

Amino Acids↗
PubMed1993

Amplification of the bacA gene confers bacitracin resistance to Escherichia coli.

An Escherichia coli genomic library was constructed in order to facilitate selection for genes which confer bacitracin resistance through amplification. One of the plasmids from the library, plasmid pXV62, provided a high level of bacitracin resistance for E. coli. Deletion and nucleotide sequence analyses of bacitracin resistance plasmid pXV62 revealed that a single open reading frame, designated the bacA gene, was sufficient for antibiotic resistance. The bacA gene mapped to approximately 67 min on the E. coli chromosome by proximity to a previously mapped locus. The deduced amino acid sequence of the bacA-encoded protein suggests an extremely hydrophobic protein of 151 amino acids, approximately 65% of which were nonpolar amino acids. E. coli cells containing plasmid pXV62 have increased isoprenol kinase activity. The physical characteristics of the deduced protein and enhanced lipid kinase activity suggest that the bacA gene may confer resistance to bacitracin by phosphorylation of undecaprenol.

Amino Acid Sequence↗
PubMed1962

Requirement of divalent metal ions for bacitracin activity.

Adler, Richard H. (University of California, Los Angeles) and John E. Snoke. Requirement of divalent metal ions for bacitracin activity. J. Bacteriol. 83:1315-1317. 1962.-The antibiotic activity of bacitracin towards Staphylococcus aureus is completely suppressed by ethylenediaminetetraacetate. The conclusion that bacitracin activity requires the presence of metal ions is supported by the demonstration that the addition of a number of divalent ions reverses the effect of ethylenediaminetetraacetate. The most active of these ions, cadmium, manganese, and zinc, directly enhance the activity of bacitracin.

Anti-Bacterial Agents↗
PubMed2005

The metallopeptide antibiotic bacitracin inhibits interleukin-12 alphabeta and beta2 secretion.

The metalloantibiotic bacitracin is a known inhibitor of protein disulfide isomerase (PDI). The disulfide-linked interleukin-12 (IL-12) alphabeta-heterodimer and beta2-homodimer forms are crucial mediators of cell-mediated immune responses and inflammatory reactions. Bacitracin was found to potently block secretion of both the alphabeta- and beta2-dimer forms of IL-12, while it did not affect secretion of the beta-monomer. This inhibition coincided with a reduction in the intracellular amount of PDI found in complex with the beta-chain during intracellular transit. Bacitracin did not affect mRNA levels of the alphabeta- and beta-chain. Similar to bacitracin, N-acetylcysteine blocked alphabeta- and beta2-secretion as well as PDI-beta-chain complex formation. Thus, blocking PDI or shifting the endoplasmic reticulum towards a more reduced status disrupts the oxidative folding pathway or assembly of IL-12 dimer forms. The assembly stage of cytokines in the endoplasmic reticulum may represent a novel target for pharmacological intervention.

Acetylcysteine↗
PubMedDate not supplied

Inhibition of resistance plasmid transfer in Escherichia coli by ionophores, chlortetracycline, bacitracin, and ionophore/antimicrobial combinations.

Medicinal feed additives bacitracin, chlortetracycline (CTC), laidlomycin, lasalocid, and salinomycin inhibited the transfer of multiresistance-conferring plasmid pBR325 (Tet(r) Amp(r) Cp(r), 6.0 kb) into selected gram-negative strains with the use of an in vitro model. High concentrations of ampicillin-sensitive competence-pretreated Escherichia coli HB 101 cells were exposed to 10% (v/v) of 1:10 dimethyl sulfoxide/agent : water containing test mixtures for 0.5 hr prior to plasmid addition and transforming conditions. Transformation was inhibited for all antimicrobials and showed a positive association wich higher concentration. Additional testing of ionophore compounds separately and in combination with bacitracin, chlortetracycline, lincomycin, roxarsone, tylosin, and virginiamycin at representative feed concentrations demonstrated 80.6% to >99.9% inhibition (P < 0.001) of resistance transfer. Bacitracin alone inhibited transformation within the range of 50-500 ppm. No increase in resistance transfer was observed when poultry-derived and reference gram-negative isolates having low or no transformation efficiency were additionally tested. The results suggest that these compounds, at relevant concentrations used in animal feed, may interfere with cell envelope-associated DNA uptake channels or other transformation competence mechanisms. Through these mechanisms, ionophores and cell membrane-interactive feed agents such as CTC and bacitracin may act to inhibit resistance transfer mechanisms within poultry and livestock.

Bacitracin↗
PubMed1988

Effect of bacitracin on binding and processing of insulin by established renal cell line.

The effect of bacitracin on the binding and processing of 125I-labeled insulin was studied in a proximal tubular epithelium-like opossum kidney cell line. This cultured cell line handles insulin in a manner comparable to the in vivo situation, which requires membrane binding, internalization, and intracellular degradation. The addition of bacitracin inhibited insulin degradation significantly and delayed the time of appearance of products in the medium (22 min) compared with control cells (14 min). Maximum total cell-associated radioactivity increased from 1.5 +/- 0.19% in the control cells to 2.5 +/- 0.17% in the treated cells. Separation of cell membrane from internalized radioactivity was achieved by acid washing and showed no change in membrane-bound radioactivity or rate of internalization, but a significant increase in intracellular radioactivity was noted. Gel-filtration chromatography revealed that this was due to an accumulation of chromatographically intact insulin. Accordingly, we conclude that bacitracin inhibits insulin degradation in cultured kidney cells by perturbing the intracellular processing of insulin, not by altering the binding or internalization of the hormone or by inhibiting the release of small degradation products. Because of the multiple actions of this agent, the exact site in these kidney cells at which intracellular degradation is inhibited remains to be established. However, in contrast to studies with lysosomes isolated from cells of other tissues, this study showed that when lysosomes isolated from rat renal cortex were exposed to bacitracin, insulin degradation was inhibited markedly (81%).

Animals↗
PubMed1986

Response of broiler chickens to addition of zinc bacitracin to diets containing salinomycin and roxarsone.

Five trials were conducted at various locations to determine the response of broiler chickens to the addition of zinc bacitracin to diets containing both salinomycin and roxarsone. Results indicate that when a combination of salinomycin and roxarsone is used as an anticoccidial, the addition of zinc bacitracin at 33 or 55 mg/kg diet will improve growth rate and feed utilization by broiler chickens. Regression of body weight and feed utilization on dietary levels of zinc bacitracin indicated that each milligram of zinc bacitracin in the diet increased the 49-day weight of broiler chickens by .92 g and reduced the feed required per gram of gain by .0012 g.

Animals↗
PubMed1999

Investigation of antistaphylococcal activity of collagen dressing containing bacitracin.

In the present paper the anti-bacterial effect of bacitracin released from the collagen-based dressing and penetrating to the Staphylococcus aureus-colonised polyurethane sponge was assessed. The bacteria-colonised sponge, regarded as the "in vitro model of an infected wound", was used as a modification of the previously utilised by us analogous experimental systems. In addition, kinetics of the penetration of bacitracin from the collagen dressing to the sponge was estimated. The results indicate that in spite of the fact that the amount of bacitracin in the polyurethane sponge exceeded the minimal bactericidal concentration (MBC), not all bacteria from the S. aureus species colonising the sponge could be killed. Moreover, it appeared that in order to efficiently eradicate the sponge-adherent staphylococci the concentration of bacitracin 50-fold higher than the MBC value must be used.

Bacitracin↗
PubMed1991

[Comparison of latex agglutination and bacitracin-SXT methods used for the identification of 142 beta-hemolytic streptococci].

We compared the latex agglutination and bacitracin-SXT methods to identify Group A Streptococci (GAS) from throat cultures. In our study all 118 GAS strains identified by latex agglutination method were found susceptible to bacitracin, 115 were found resistant and 3 were susceptible to SXT. All beta hemolytic streptococci rather than GAS were found resistant to bacitracin. As a result bacitracin method is found valuable in rutin studies in GAS identification.

Bacitracin↗