Journal articles: 'Bacitracin'

1

&NA;. "Bacitracin see Polymixin B + bacitracin." Reactions Weekly &NA;, no. 327 (November 1990): 4. http://dx.doi.org/10.2165/00128415-199003270-00011.

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Blackard, W. G., C. Ludeman, and J. Stillman. "Role of hepatocyte plasma membrane in insulin degradation." American Journal of Physiology-Endocrinology and Metabolism 248, no. 2 (February 1, 1985): E194—E202. http://dx.doi.org/10.1152/ajpendo.1985.248.2.e194.

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An important role of the cell membrane in insulin degradation by cultured rat hepatocytes is supported by studies using the surface-active antibiotic bacitracin. Bacitracin inhibited degradation of cell-associated insulin (both randomly and A14 labeled) by 80–90% at 15 degrees C and by 60% at 37 degrees C. At 37 degrees C, inhibition of degradation was observed only with bacitracin present during dissociation and was accompanied by a compensatory increase in release of trichloroacetic acid (TCA)-precipitable insulin. This profile suggests inhibition of insulin degradation on the membrane after either primary binding or diacytosis (endocytosis-reverse endocytosis). In contrast, at 15 degrees C, bacitracin's inhibitory effect was greater with the antibiotic present during association and was not accompanied by a compensatory increase in TCA-precipitable insulin. This profile was compatible with inhibition of partial cleavage of insulin on the membrane. Internalization and degradation through chloroquine-sensitive pathways may be required to complete degradation at this temperature because chloroquine exhibited an inhibitory effect on insulin degradation equally potent to that of bacitracin at 15 degrees C (no effect at 37 degrees C).

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 693 (March 1998): 6. http://dx.doi.org/10.2165/00128415-199806930-00015.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 723 (October 1998): 7. http://dx.doi.org/10.2165/00128415-199807230-00020.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1135 (January 2007): 9. http://dx.doi.org/10.2165/00128415-200711350-00029.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1356 (June 2011): 9–10. http://dx.doi.org/10.2165/00128415-201113560-00026.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 441 (March 1993): 6. http://dx.doi.org/10.2165/00128415-199304410-00016.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 668 (September 1997): 6. http://dx.doi.org/10.2165/00128415-199706680-00015.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 828 (November 2000): 8. http://dx.doi.org/10.2165/00128415-200008280-00011.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1218 (September 2008): 7–8. http://dx.doi.org/10.2165/00128415-200812180-00020.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1223 (October 2008): 7. http://dx.doi.org/10.2165/00128415-200812230-00022.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1085 (January 2006): 9. http://dx.doi.org/10.2165/00128415-200610850-00027.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1257 (June 2009): 10. http://dx.doi.org/10.2165/00128415-200912570-00029.

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&NA;. "Bacitracin." Reactions Weekly &NA;, no. 333 (January 1991): 4. http://dx.doi.org/10.2165/00128415-199103330-00013.

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15

&NA;. "Bacitracin see Neomycin/bacitracin/polymixin B." Reactions Weekly &NA;, no. 335 (January 1991): 4. http://dx.doi.org/10.2165/00128415-199103350-00011.

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&NA;. "Neomycin/bacitracin." Reactions Weekly &NA;, no. 399 (May 1992): 10. http://dx.doi.org/10.2165/00128415-199203990-00045.

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&NA;. "Bacitracin/colistin." Reactions Weekly &NA;, no. 1081 (December 2005): 8. http://dx.doi.org/10.2165/00128415-200510810-00023.

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&NA;. "Bacitracin/neomycin." Reactions Weekly &NA;, no. 1082 (December 2005): 8. http://dx.doi.org/10.2165/00128415-200510820-00019.

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19

&NA;. "Bacitracin + clioquinol." Reactions Weekly &NA;, no. 348 (April 1991): 5. http://dx.doi.org/10.2165/00128415-199103480-00008.

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20

Brod, Bruce A. "Bacitracin Anaphylaxis." American Journal of Contact Dermatitis 7, no. 3 (September 1996): 193. http://dx.doi.org/10.1097/01634989-199609000-00015.

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Brod, Bruce A. "Bacitracin Anaphylaxis." Dermatitis 7, no. 3 (September 1996): 193. http://dx.doi.org/10.1097/01206501-199609000-00015.

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BROD, B. "Bacitracin anaphylaxis." American Journal of Contact Dermatitis 7, no. 3 (September 1996): 193. http://dx.doi.org/10.1016/s1046-199x(96)90014-7.

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23

Ohki, Reiko, Kozue Tateno, Youji Okada, Haruo Okajima, Kei Asai, Yoshito Sadaie, Makiko Murata, and Toshiko Aiso. "A Bacitracin-Resistant Bacillus subtilis Gene Encodes a Homologue of the Membrane-Spanning Subunit of the Bacillus licheniformis ABC Transporter." Journal of Bacteriology 185, no. 1 (January 1, 2003): 51–59. http://dx.doi.org/10.1128/jb.185.1.51-59.2003.

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ABSTRACT Bacitracin is a peptide antibiotic nonribosomally produced by Bacillus licheniformis. The bcrABC genes which confer bacitracin resistance to the bacitracin producer encode ATP binding cassette (ABC) transporter proteins, which are hypothesized to pump out bacitracin from the cells. Bacillus subtilis 168, which has no bacitracin synthesizing operon, has several genes homologous to bcrABC. It was found that the disruption of ywoA, a gene homologous to bcrC, resulted in hypersensitivity to bacitracin. Resistance to other drugs such as surfactin, iturin A, vancomycin, tunicamycin, gramicidin D, valinomycin and several cationic dyes were not changed in the ywoA disruptant. Spontaneous bacitracin-resistant mutants (Bcr-1 and -2) isolated in the presence of bacitracin have a single base substitution from A to G in the ribosome binding region. Northern hybridization analysis and determination of the expression of ywoA-LacZ transcriptional fusion gene revealed that the transcription of the ywoA gene was dependent on extracytoplasmic function (ECF) σ factors σM and σX. Preincubation of wild-type cells in the presence of a low concentration of bacitracin induced increased resistance to bacitracin about two- to threefold, although the mechanism of this induction has not yet been elucidated. It has been reported that a commercially available bacitracin is a mixture of several components and also contains impurity. Bacitracin A was purified by reverse phase high-performance liquid chromatography (HPLC). Similar results were obtained with bacitracin A as those with crude bacitracin, indicating that contaminating substances were not responsible for the results obtained in this study.

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Tsuda, Hiromasa, Yoshihisa Yamashita, Yukie Shibata, Yoshio Nakano, and Toshihiko Koga. "Genes Involved in Bacitracin Resistance in Streptococcus mutans." Antimicrobial Agents and Chemotherapy 46, no. 12 (December 2002): 3756–64. http://dx.doi.org/10.1128/aac.46.12.3756-3764.2002.

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ABSTRACT Streptococcus mutans is resistant to bacitracin, which is a peptide antibiotic produced by certain species of Bacillus. The purpose of this study was to clarify the bacitracin resistance mechanism of S. mutans. We cloned and sequenced two S. mutans loci that are involved in bacitracin resistance. The rgp locus, which is located downstream from rmlD, contains six rgp genes (rgpA to rgpF) that are involved in rhamnose-glucose polysaccharide (RGP) synthesis in S. mutans. The inactivation of RGP synthesis in S. mutans resulted in an approximately fivefold-higher sensitivity to bacitracin relative to that observed for the wild-type strain Xc. The second bacitracin resistance locus comprised four mbr genes (mbrA, mbrB, mbrC, and mbrD) and was located immediately downstream from gtfC, which encodes the water-insoluble glucan-synthesizing enzyme. Although the bacitracin sensitivities of mutants that had defects in flanking genes were similar to that of the parental strain Xc, mutants that were defective in mbrA, mbrB, mbrC, or mbrD were about 100 to 120 times more sensitive to bacitracin than strain Xc. In addition, a mutant that was defective in all of the mbrABCD genes and rgpA was more sensitive to bacitracin than either the RGP or Mbr mutants. We conclude that RGP synthesis is related to bacitracin resistance in S. mutans and that the mbr genes modulate resistance to bacitracin via an unknown mechanism that is independent of RGP synthesis.

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Manson, Janet M., Stefanie Keis, John M. B. Smith, and Gregory M. Cook. "Acquired Bacitracin Resistance in Enterococcus faecalis Is Mediated by an ABC Transporter and a Novel Regulatory Protein, BcrR." Antimicrobial Agents and Chemotherapy 48, no. 10 (October 2004): 3743–48. http://dx.doi.org/10.1128/aac.48.10.3743-3748.2004.

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ABSTRACT Bacitracin resistance (bacitracin MIC, ≥256 μg ml−1) has been reported in Enterococcus faecalis, and in the present study we report on the genetic basis for this resistance. Mutagenesis was carried out with transposon Tn917 to select for E. faecalis mutants with decreased resistance to bacitracin. Two bacitracin-sensitive mutants (MICs, 32 μg ml−1) were obtained and Tn917 insertions were mapped to genes designated bcrA and bcrB. The amino acid sequences of BcrA (ATP-binding domain) and BrcB (membrane-spanning domain) are predicted to constitute a homodimeric ATP-binding cassette (ABC) transporter, the function of which is essential for bacitracin resistance in E. faecalis. The bcrA and bcrB genes were organized in an operon with a third gene, bcrD, that had homology to undecaprenol kinases. Northern analysis demonstrated that bcrA, bcrB, and bcrD were transcribed as a polycistronic message that was induced by increasing concentrations of bacitracin but not by other cell wall-active antimicrobials (e.g., vancomycin). Upstream of the bcrABD operon was a putative regulatory gene, bcrR. The bcrR gene was expressed constitutively, and deletion of bcrR resulted in a bacitracin-sensitive phenotype. No bcrABD expression was observed in a bcrR mutant, suggesting that BcrR is an activator of genes essential for bacitracin resistance (i.e., bcrABD). The bacitracin resistance genes were found to be located on a plasmid that transferred at a high frequency to E. faecalis strain JH2-2. This report represents the first description of genes that are essential for acquired bacitracin resistance in E. faecalis.

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Han, Xiaoyan, Xiang-Dang Du, Luke Southey, Dieter M. Bulach, Torsten Seemann, Xu-Xia Yan, Trudi L. Bannam, and Julian I. Rood. "Functional Analysis of a Bacitracin Resistance Determinant Located on ICECp1, a Novel Tn916-Like Element from a Conjugative Plasmid in Clostridium perfringens." Antimicrobial Agents and Chemotherapy 59, no. 11 (August 17, 2015): 6855–65. http://dx.doi.org/10.1128/aac.01643-15.

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ABSTRACTBacitracins are mixtures of structurally related cyclic polypeptides with antibiotic properties. They act by interfering with the biosynthesis of the bacterial cell wall. In this study, we analyzed an avian necrotic enteritis strain ofClostridium perfringensthat was resistant to bacitracin and produced NetB toxin. We identified a bacitracin resistance locus that resembled a bacitracin resistance determinant fromEnterococcus faecalis. It contained the structural genesbcrABDand a putative regulatory gene,bcrR. Mutagenesis studies provided evidence that bothbcrAandbcrBare essential for bacitracin resistance, and that evidence was supported by the results of experiments in which the introduction of both thebcrAandbcrBgenes into a bacitracin-susceptibleC. perfringensstrain was required to confer bacitracin resistance. The wild-type strain was shown to contain at least three large, putatively conjugative plasmids, and thebcrRABDlocus was localized to an 89.7-kb plasmid, pJIR4150. This plasmid was experimentally shown to be conjugative and was sequenced. The sequence revealed that it also carries atpeLtoxin gene and is related to the pCW3 family of conjugative antibiotic resistance and toxin plasmids fromC. perfringens. Thebcrgenes were located on a genetic element, ICECp1, which is related to the Tn916family of integrative conjugative elements (ICEs). ICECp1appears to be the first Tn916-like element shown to confer bacitracin resistance. In summary, we identified in a toxin-producingC. perfringensstrain a novel mobile bacitracin resistance element which was experimentally shown to be essential for bacitracin resistance and is carried by a putative ICE located on a conjugative plasmid.

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Smith, Janet D., and Gordon T. Bolger. "Selective inhibition of [3H]nitrendipine binding to brain and cardiac membranes by bacitracin." Canadian Journal of Physiology and Pharmacology 67, no. 12 (December 1, 1989): 1591–95. http://dx.doi.org/10.1139/y89-255.

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The effects of bacitracin were investigated on [3H]nitrendipine binding to rat brain and cardiac membranes in a low ionic strength (5 mM Tris–HCl) buffer. Bacitracin inhibited [3H]nitrendipine binding to rat brain and cardiac membranes with IC50 values of 400 ± 100 and 4600 ± 400 μg/mL, respectively. Scatchard analysis in brain membranes revealed that bacitracin inhibited [3H]nitrendipine binding primarily by reducing the Bmax but also by producing a small increase in the Kd. In brain membranes, Na+ (100 mM) and Ca2+ (2 mM) reduced the potency of bacitracin to inhibit [3H]nitrendipine binding by approximately sixfold with IC50 values of 2600 ± 300 and 2100 ± 400 μg/mL observed for bacitracin in the presence of 100 mM Na+ and 2 mM Ca2+, respectively. The EC50 values for the effects of Na+ and Ca2+ were 800 ± 200 μM and 25 ± 5 mM. K+, Mg2+, choline, and increasing the assay buffer of Tris–HCl to 50 mM also decreased the inhibition of [3H]nitrendipine binding by bacitracin. These results suggest that bacitracin specifically modulates [3H]nitrendipine binding in a cation-dependent manner and that brain and cardiac dihydropyridine binding sites are either biochemically different or exist in a different membrane environment.Key words: bacitracin, [3H]nitrendipine, brain, heart.

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Cao, Min, and John D. Helmann. "Regulation of the Bacillus subtilis bcrC Bacitracin Resistance Gene by Two Extracytoplasmic Function σ Factors." Journal of Bacteriology 184, no. 22 (November 15, 2002): 6123–29. http://dx.doi.org/10.1128/jb.184.22.6123-6129.2002.

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ABSTRACT Bacitracin resistance is normally conferred by either of two major mechanisms, the BcrABC transporter, which pumps out bacitracin, or BacA, an undecaprenol kinase that provides C55-isoprenyl phosphate by de novo synthesis. We demonstrate that the Bacillus subtilis bcrC (ywoA) gene, encoding a putative bacitracin transport permease, is an important bacitracin resistance determinant. A bcrC mutant strain had an eightfold-higher sensitivity to bacitracin. Expression of bcrC initiated from a single promoter site that could be recognized by either of two extracytoplasmic function (ECF) σ factors, σX or σM. Bacitracin induced expression of bcrC, and this induction was dependent on σM but not on σX. Under inducing conditions, expression was primarily dependent on σM. As a consequence, a sigM mutant was fourfold more sensitive to bacitracin, while the sigX mutant was only slightly sensitive. A sigX sigM double mutant was similar to a bcrC mutant in sensitivity. These results support the suggestion that one function of B. subtilis ECF σ factors is to coordinate antibiotic stress responses.

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Beckman, Joshua M., Ernest K. Amankwah, Lisa L. Tetreault, Sharon A. Perlman, and Gerald F. Tuite. "Complications associated with bacitracin powder in surgical wounds." Journal of Neurosurgery: Pediatrics 16, no. 6 (December 2015): 719–25. http://dx.doi.org/10.3171/2015.4.peds14699.

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OBJECT There has been renewed interest in the application of concentrated antibiotic powder to surgical wounds as a method to decrease infection rates. While there is substantial medical literature describing the effectiveness and complications associated with vancomycin and gentamycin powders, very little has been reported regarding the safety and effectiveness of bacitracin powder in surgical wounds. In this paper the authors report their detailed analysis of potential bacitracin powder-related complications in a population of pediatric patients who underwent shunt surgery. METHODS A detailed retrospective analysis was completed of all CSF shunt surgeries performed by the corresponding author at a large children’s hospital between 2001 and 2013. This cohort consisted of many patients who were the subject of a previous report that showed the use of bacitracin powder in shunt wounds potentially decreased infection rates. Data were collected regarding the most common known complications of bacitracin, i.e., anaphylaxis, wound healing difficulties, and renal dysfunction. Data were stratified by typical demographic, medical, and surgical variables, including whether bacitracin powder was applied to wounds prior to closure. RESULTS A total of 597 patients were reviewed in the analysis: 389 underwent surgery without bacitracin powder and 208 had concentrated bacitracin powder applied to the wounds prior to closure. The application of bacitracin powder was not associated with anaphylaxis (n = 0 both groups) or with an increase in wound breakdown (n = 5 in the control group, n = 0 in the bacitracin powder group) or renal dysfunction (creatinine/estimated glomerular filtration rate) using both comparative and multivariate analyses between the 2 groups. The sample size evaluating renal function was significantly lower (range 6–320) than that of anaphylaxis and wound breakdown analysis because only clinical values acquired during the routine care of these patients were available for analysis. The only significant difference in demographics was the more frequent use of intrathecal vancomycin and gentamycin in patients who received bacitracin powder (n = 1 for controls, n = 21 for bacitracin powder). In the multivariate analysis, only 1 factor, surgery performed on a premature infant within the first 3 months of life, was independently associated with a change in creatinine at 3 months (creatinine decreased by 0.18) compared with the level before surgery (p < 0.0001). Bacitracin powder was not a significant factor. CONCLUSIONS To the authors’ knowledge, this is the first study to systematically analyze the potential complications of concentrated bacitracin powder applied to surgical wounds. The use of topical bacitracin powder in CSF shunt wounds was not associated with anaphylaxis, wound breakdown, or renal dysfunction. Further study using standardized protocols is necessary before widespread use can be recommended.

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&NA;. "Polymixin B + bacitracin." Reactions Weekly &NA;, no. 327 (November 1990): 8. http://dx.doi.org/10.2165/00128415-199003270-00043.

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31

&NA;. "Bacitracin/corticosteroids/neomycin." Reactions Weekly &NA;, no. 1291 (March 2010): 10. http://dx.doi.org/10.2165/00128415-201012910-00029.

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Podlesek, Z., and A. Comino. "Antagonists of bacitracin." Letters in Applied Microbiology 19, no. 2 (August 1994): 102–4. http://dx.doi.org/10.1111/j.1472-765x.1994.tb00916.x.

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Wang, Xitao, and Mohammad Asghar. "Protein disulfide isomerase regulates renal AT1 receptor function and blood pressure in rats." American Journal of Physiology-Renal Physiology 313, no. 2 (August 1, 2017): F461—F466. http://dx.doi.org/10.1152/ajprenal.00580.2016.

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The role and mechanism of renal protein disulfide isomerase (PDI) in blood pressure regulation has not been tested before. Here, we test this possibility in Sprague-Dawley rats. Rats were treated with PDI inhibitor bacitracin (100 mg·kg−1 ip·day−1 for 14 days), and then blood pressure and renal angiotensin II type 1 (AT1) receptor function were determined in anesthetized rats. Renal AT1 receptor function was determined as the ability of candesartan (an AT1 receptor blocker) to increase diuresis and natriuresis. A second set of vehicle- and bacitracin-treated rats was used to determine biochemical parameters. Systolic blood pressure as well as diastolic blood pressure increased in bacitracin-treated compared with vehicle-treated rats. Compared with vehicle, bacitracin-treated rats showed increased diuresis and natriuresis in response to candesartan (10-µg iv bolus dose) suggesting higher AT1 receptor function in these rats. These were associated with higher renin activities in the plasma and renal tissues. Furthermore, urinary 8-isoprostane and kidney injury molecule-1 levels were higher and urinary antioxidant capacity was lower in bacitracin-treated rats. Renal protein carbonyl and nitrotyrosine levels also were higher in bacitracin- compared with vehicle-treated rats, suggesting oxidative stress burden in bacitracin-treated rats. Moreover, PDI activity decreased and its protein levels increased in renal tissues of bacitracin-treated rats. Also, nuclear levels of Nrf2 transcription factor, which regulates redox homeostasis, were decreased in bacitracin-treated rats. Furthermore, tissue levels of Keap1, an Nrf2 inhibitory molecule, and tyrosine 216-phosphorylated GSK3β protein, an Nrf2 nuclear export protein, were increased in bacitracin-treated rats. These results suggest that renal PDI by regulating Keap1-Nrf2 pathway acts as an antioxidant, maintaining redox balance, renal AT1 receptor function, and blood pressure in rats.

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HAAVIK, H. I. "Studies on the Formation of Bacitracin by Bacillus licheniformis: Effect of Glucose." Microbiology 81, no. 2 (February 1, 2000): 383–90. http://dx.doi.org/10.1099/00221287-81-2-383.

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Summary: The production of bacitracin by Bacillus licheniformis closely paralleled growth in a synthetic medium without glucose. Glucose inhibited bacitracin production during the first hours of growth, whereas growth was not affected. Bacitracin was produced mainly during the later stages of growth. Formation of bacitracin was apparently not under catabolite repression control by glucose since the inhibitory effect of glucose upon the early bacitracin production was prevented by neutralizing the culture fluid with CaCO3. The inhibitory effect of glucose may be due to the low pH created by its metabolism. Addition of 0.5% glucose markedly increased the maximum titre of bacitracin. This stimulation could also be due to the effect of glucose metabolism upon the pH of the medium. The observation that peptide antibiotics are produced mainly after growth is not always true; in appropriate media they might also be produced during the phase of rapid growth.

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Zhu, Ziyu, Leonie Schnell, Bastian Müller, Martin Müller, Panagiotis Papatheodorou, and Holger Barth. "The Antibiotic Bacitracin Protects Human Intestinal Epithelial Cells and Stem Cell-Derived Intestinal Organoids from Clostridium difficile Toxin TcdB." Stem Cells International 2019 (August 5, 2019): 1–8. http://dx.doi.org/10.1155/2019/4149762.

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Bacitracin is an established antibiotic for local application and inhibits the cell wall synthesis of Gram-positive bacteria. Recently, we discovered a completely different mode of action of bacitracin and reported that this drug protects human cells from intoxication by a variety of medically relevant bacterial protein toxins including CDT, the binary actin ADP-ribosylating toxin of Clostridium (C.) difficile. Bacitracin prevents the transport of CDT into the cytosol of target cells, most likely by inhibiting the transport function of the binding subunit of this toxin. Here, we tested the effect of bacitracin towards TcdB, a major virulence factor of C. difficile contributing to severe C. difficile-associated diseases (CDAD) including pseudomembranous colitis. Bacitracin protected stem cell-derived human intestinal organoids as well as human gut epithelial cells from intoxication with TcdB. Moreover, it prevented the TcdB-induced disruption of epithelia formed by gut epithelium cells in vitro and maintained the barrier function as detected by measuring transepithelial electrical resistance (TEER). In the presence of bacitracin, TcdB was not able reach its substrate Rac1 in the cytosol of human epithelial cells, most likely because its pH-dependent transport across cell membranes into the cytosol is decreased by bacitracin. In conclusion, in addition to its direct antibiotic activity against C. difficile and its inhibitory effect towards the toxin CDT, bacitracin neutralizes the exotoxin TcdB of this important pathogenic bacterium.

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Netland, Peter A., James E. Baumgartner, and Brian T. Andrews. "Intraoperative Anaphylaxis after Irrigation with Bacitracin: Case Report." Neurosurgery 21, no. 6 (April 1, 1987): 927–28. http://dx.doi.org/10.1227/00006123-198712000-00026.

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Abstract We report a case of anaphylaxis caused by irrigation with a bacitracin solution during lumbar laminectomy. The patient had been exposed to bacitracin during a previous anterior cervical discectomy. We recommend avoiding the use of irrigation solutions containing bacitracin in patients with previous systemic exposure to this antibiotic.

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Lin, Kuei-Hung, and Yu-Hsiang Yu. "Evaluation of Bacillus licheniformis-Fermented Feed Additive as an Antibiotic Substitute: Effect on the Growth Performance, Diarrhea Incidence, and Cecal Microbiota in Weaning Piglets." Animals 10, no. 9 (September 14, 2020): 1649. http://dx.doi.org/10.3390/ani10091649.

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This study investigated the potential of a Bacillus licheniformis-fermented feed additive (BLF) as an antibiotic substitute in weaning piglets. Ninety-six crossbred piglets were randomly allotted into four treatments with three replicate pens per treatment and eight pigs per pen. Piglets were fed diets as follows: a basal diet as control, a basal diet supplemented with bacitracin (30 mg/kg of bacitracin methylene disalicylate), a basal diet supplemented with BLF (1 g/kg of the Bacillus licheniformis-fermented feed additive), and a basal diet supplemented with bacitracin and BLF (15 mg/kg of bacitracin methylene disalicylate and 0.5 g/kg of the Bacillus licheniformis-fermented feed additive). The results showed that replacing all or half the bacitracin with BLF both reduced the incidence of diarrhea in weaning piglets from day 1 to 14. Principal coordinates analysis and a species abundance heat map showed that distinct clusters were formed between groups. Replacing all the bacitracin with BLF reduced bacterial evenness in the cecal digesta of weaning piglets, while the inhibitory effect on bacterial evenness was reversed in the group treated with bacitracin in combination with BLF. These results indicated that the half replacement of bacitracin with BLF was able to decrease the incidence of diarrhea and modify cecal microbiota composition in weaning piglets, suggesting that a Bacillus licheniformis-fermented feed additive has good potential as a suitable alternative to antibiotics use in the swine industry.

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Harel, Yael Meller, Adriana Bailone, and Eitan Bibi. "Resistance to Bacitracin as Modulated by an Escherichia coli Homologue of the Bacitracin ABC Transporter BcrC Subunit from Bacillus licheniformis." Journal of Bacteriology 181, no. 19 (October 1, 1999): 6176–78. http://dx.doi.org/10.1128/jb.181.19.6176-6178.1999.

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ABSTRACT A small open reading frame from the Escherichia colichromosome, bcrC EC, encodes a homologue to the BcrC subunit of the bacitracin permease from Bacillus licheniformis. We show that disruption of the chromosomalbcrC EC gene causes bacitracin sensitivity and, conversely, that BcrCEC confers bacitracin resistance when expressed from a multicopy plasmid.

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Wang, Lin, Liu Liu, and Xiaotong Zhou. "Bacitracin-Ag Nanoclusters as a Novel Antibacterial Agent Combats Shigella flexneri by Disrupting Cell Membrane and Inhibiting Biofilm Formation." Nanomaterials 11, no. 11 (November 1, 2021): 2928. http://dx.doi.org/10.3390/nano11112928.

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A novel nanomaterial Bacitracin-Ag Nanoclusters (Bacitracin-AgNCs) was formed to achieve a better antibacterial effect on Shigella flexneri which poses a serious threat to human health. In the current study, X-ray photoelectron spectrometer (XPS), Fourier transform infrared (FTIR), field-emission scanning electron microscopy (FESEM), high resolution transmission electron microscopy (HR-TEM) and thermal gravimetric analysis (TGA) were used to characterize the properties of composited Bacitracin-AgNCs. Furthermore, the inhibitory effects of Bacitracin-AgNCs against S. flexneri were explored, and the inhibition mechanism was discussed in terms of its aspects of cell membrane ravage, ATPase activity decline and biofilm inhibition. The results reveal that the minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) of Bacitracin-AgNCs against S. flexneri were 0.03 mg/mL and 4 mg/mL. Bacitracin-AgNCs may cause irreversible impairment to cells and greatly change the cell morphology. The cell membrane integrity of S. flexneri was destroyed with changes in the characteristics of membrane permeability and intracellular substances leakage. Moreover, our study further proved that Bacitracin-AgNCs significantly inhibited the formation of S. flexneri biofilms and reduced the number of viable bacteria in biofilm. These findings provide a potential method for the exploitation of organic composite nanomaterials as a novel antimicrobial agent and its application in the food industry.

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Chapnick, Edward K., Jeremy D. Gradon, Barry Kreiswirth, Larry I. Lutwick, Benjamin C. Schaffer, Thomas D. Schiano, and Michael H. Levi. "Comparative Killing Kinetics of Methicillin-Resistant Staphylococcus aureus by Bacitracin or Mupirocin." Infection Control & Hospital Epidemiology 17, no. 3 (March 1996): 178–80. http://dx.doi.org/10.1017/s0195941700006548.

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AbstractThe 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 μg/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 μg/mL). Bacitracin should be considered further for in vivo studies because of enhanced bacteriocidal effect and lower cost.

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Santativongchai, Pitchaya, Phitsanu Tulayakul, Yinduo Ji, and Byeonghwa Jeon. "Synergistic Potentiation of Antimicrobial and Antibiofilm Activities of Penicillin and Bacitracin by Octyl Gallate, a Food-Grade Antioxidant, in Staphylococcus epidermidis." Antibiotics 11, no. 12 (December 8, 2022): 1775. http://dx.doi.org/10.3390/antibiotics11121775.

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Staphylococcus epidermidis is a major nosocomial pathogen that frequently forms biofilms on indwelling medical devices. This study aimed to investigate the synergistic antimicrobial and antibiofilm activities of octyl gallate (OG) in combination with penicillin and bacitracin against S. epidermidis. Antimicrobial synergy was assessed by conducting checkerboard titration assays, and antibiofilm activity was determined with biofilm assays and fluorescence microscopy analysis. The presence of 8 µg/mL of OG increased both the bacteriostatic and bactericidal activities of penicillin and bacitracin against S. epidermidis. It lowered the minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) of penicillin by eight-fold and those of bacitracin by four-fold. Moreover, when used with penicillin or bacitracin, OG significantly decreased the level of biofilm production by preventing microcolony formation. Furthermore, OG significantly permeabilized the bacterial cell wall, which may explain its antimicrobial synergy with penicillin and bacitracin. Together, these results demonstrate that OG, a food-grade antioxidant, can be potentially used as a drug potentiator to enhance the antimicrobial and antibiofilm activities of penicillin and bacitracin against S. epidermidis.

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Andrews, Barry J., Alexandru C. Vasile-Bugarin, Rhodica P. Vasiliu, Gheorge H. Jipa, Dan Panitescu, and Jorgen R. Ronnevig. "Chemotherapy for Giardiasis: Randomized Clinical Trial of Bacitracin, Bacitracin Zinc, and a Combination of Bacitracin Zinc with Neomycin." American Journal of Tropical Medicine and Hygiene 52, no. 4 (April 1, 1995): 318–21. http://dx.doi.org/10.4269/ajtmh.1995.52.318.

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Webster, Gregory K. "Liquid Chromatographic Analysis of Bacitracin Methylene Disalicylate in Feed." Journal of AOAC INTERNATIONAL 80, no. 4 (July 1, 1997): 732–36. http://dx.doi.org/10.1093/jaoac/80.4.732.

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Abstract Because of its peptide structure, bacitracin is not chemically distinct from many matrixes such as feeds or residue samples. Thus, bacitracin must be isolated from the matrix components or chemically altered to form a distinct component. Because of the complexity of this problem, bacitracin is still analyzed almost exclusively by microbiological methods. However, advances in solid-phase extraction has made sample isolation from the matrix much more practical. In this investigation both strong-cation exchange and C8 columns were used to isolate bacitracin for liquid chromatographic (LC) analysis. Results of both LC and microbiological analyses are compared.

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Aslanli, Aysel, Maksim Domnin, Nikolay Stepanov, and Elena Efremenko. "“Universal” Antimicrobial Combination of Bacitracin and His6-OPH with Lactonase Activity, Acting against Various Bacterial and Yeast Cells." International Journal of Molecular Sciences 23, no. 16 (August 20, 2022): 9400. http://dx.doi.org/10.3390/ijms23169400.

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The effect of Bacitracin as an antibiotic acting against Gram-positive bacterial cells was evaluated in combination with hexahistidine-containing organophosphate hydrolase (His6-OPH), possessing lactonase activity against various N-acylhomoserine lactones produced by most Gram-negative bacteria as quorum-sensing molecules. The molecular docking technique was used to obtain in silico confirmation of possible interactions between molecules of His6-OPH and Bacitracin as well as the absence of a significant influence of such interactions on the enzymatic catalysis. The in vitro experiments showed a sufficient catalytic efficiency of action of the His6-OPH/Bacitracin combination as compared to the native enzyme. The notable improvement (up to 3.3 times) of antibacterial efficiency of Bacitracin was revealed in relation to Gram-negative bacteria when it was used in combination with His6-OPH. For the first time, the action of the Bacitracin with and without His6-OPH was shown to be effective against various yeast strains, and the presence of the enzyme increased the antibiotic effect up to 8.5 times. To estimate the role of the enzyme in the success of His6-OPH/Bacitracin with yeast, in silico experiments (molecular docking) with various fungous lactone-containing molecules were undertaken, and the opportunity of their enzymatic hydrolysis by His6-OPH was revealed in the presence and absence of Bacitracin.

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Podlesek, Zdravko, Blagajana Herzog, and Aleksandra Comino. "Amplification of bacitracin transporter genes in the bacitracin producing Bacillus licheniformis." FEMS Microbiology Letters 157, no. 1 (January 17, 2006): 201–5. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12774.x.

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Stanley Chibuzor Ikpa, Precious Chukwuemeka Isima, Chibuzo Nwokafor, Obinna Sixtus Ekwem, Roland Oghenenyerhovwo Udumebraye, Tochi Ogbu Obasi, Hope Olileanya Nwaobia, et al. "Effects of varied culture conditions on crude bacitracin produced by Bacillus subtilis isolated from the soil." Magna Scientia Advanced Biology and Pharmacy 8, no. 1 (January 30, 2023): 001–8. http://dx.doi.org/10.30574/msabp.2023.8.1.0095.

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Aim: To determine the effects subjecting Bacillus subtilis to different cultural conditions will have on the crude Bacitracin produced in inhibiting the growth of known susceptible organisms. Method: Bacillus subtilis known to be a bacitracin producer was isolated from the soil and identified. The isolate was used to produce bacitracin under various culture conditions with peptone water serving as a basal fermentation medium. The resultant crude bacitracin produced was checked for its antimicrobial activity against Staphylococcus aureus by using the agar well diffusion method. Culture conditions varied were the addition of glycerol, arabinose, fructose, mannose, sucrose, urea, MgSO4, CaCO3, KCl, sodium citrate, and the adjustment of initial pH at pH 5, 6, 8 and 9. Bacitracin production was done at 37 oC for 4 days in an orbital shaker incubator rotating at 150rpm. Result: The antimicrobial activity against the test organism (Staphylococcus aureus) was determined by the mm of the zone of inhibition, with the best result obtained from the addition of glycerol (14 mm) and the least zone of inhibition was observed from the addition of MgSO4 (3 mm). Also, pH 8 produced the best result (20 mm), while at pH 5, the antimicrobial activity of the crude bacitracin was reduced (14 mm). Conclusion: Bacitracin produced from Bacillus subtilis under various culture conditions has antimicrobial effect against Staphylococcus aureus. The highest antimicrobial activities can be gotten by the addition of glycerol and by raising the initial pH of the basal broth to pH 8 while that produced by addition of MgSO4 will have the lowest antimicrobial effect.

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&NA;. "Neomycin/bacitracin/polymixin B." Reactions Weekly &NA;, no. 335 (January 1991): 6. http://dx.doi.org/10.2165/00128415-199103350-00030.

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&NA;. "Clioquinol see Bacitracin + clioquinol." Reactions Weekly &NA;, no. 348 (April 1991): 6. http://dx.doi.org/10.2165/00128415-199103480-00018.

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&NA;. "Neomycin/bacitracin/polymyxin B." Reactions Weekly &NA;, no. 989 (February 2004): 12. http://dx.doi.org/10.2165/00128415-200409890-00034.

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Dyck, E. D., and P. Vadas. "Anaphylaxis to topical bacitracin." Allergy 52, no. 8 (August 1997): 870–71. http://dx.doi.org/10.1111/j.1398-9995.1997.tb02160.x.

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Journal articles on the topic 'Bacitracin'

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