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Journal articles on the topic 'Evernimicin'

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Published: 10 December 2022
Last updated: 29 January 2023

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1

McNicholas, Paul M., David J. Najarian, Paul A. Mann, David Hesk, Roberta S. Hare, Karen J. Shaw, and Todd A. Black. "Evernimicin Binds Exclusively to the 50S Ribosomal Subunit and Inhibits Translation in Cell-Free Systems Derived from both Gram-Positive and Gram-Negative Bacteria." Antimicrobial Agents and Chemotherapy 44, no. 5 (May 1, 2000): 1121–26. http://dx.doi.org/10.1128/aac.44.5.1121-1126.2000.

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ABSTRACT Evernimicin (SCH 27899) is a new antibiotic with activity against a wide spectrum of gram-positive bacteria and activity against some gram-negative bacteria. Previous metabolic labeling studies indicated that evernimicin specifically inhibited protein synthesis inStaphylococcus aureus. Using a susceptibleEscherichia coli strain, we demonstrated that evernimicin also inhibited protein synthesis in E. coli. In cell-free translation assays with extracts from either E. coli orS. aureus, evernimicin had a 50% inhibitory concentration of approximately 125 nM. In contrast, cell-free systems derived from wheat germ and rabbit reticulocytes were inhibited only by very high levels of evernimicin. Evernimicin did not promote transcript misreading. [14C]evernimicin specifically bound to the 50S subunit from E. coli. Nonlinear regression analysis of binding data generated with 70S ribosomes from E. coli andS. aureus and 50S subunits from E. colireturned dissociation constants of 84, 86, and 160 nM, respectively. In binding experiments, performed in the presence of excess quantities of a selection of antibiotics known to bind to the 50S subunit, only the structurally similar drug avilamycin blocked binding of [14C]evernimicin to ribosomes.
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2

Adrian, Peter V., Wenjun Zhao, Todd A. Black, Karen J. Shaw, Roberta S. Hare, and Keith P. Klugman. "Mutations in Ribosomal Protein L16 Conferring Reduced Susceptibility to Evernimicin (SCH27899): Implications for Mechanism of Action." Antimicrobial Agents and Chemotherapy 44, no. 3 (March 1, 2000): 732–38. http://dx.doi.org/10.1128/aac.44.3.732-738.2000.

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ABSTRACT A clinical isolate of Streptococcus pneumoniae (SP#5) that showed decreased susceptibility to evernimicin (MIC, 1.5 μg/ml) was investigated. A 4,255-bp EcoRI fragment cloned from SP#5 was identified by its ability to transform evernimicin-susceptibleS. pneumoniae R6 (MIC, 0.03 μg/ml) such that the evernimicin MIC was 1.5 μg/ml. Nucleotide sequence analysis of this fragment revealed that it contained portions of the S10-spc ribosomal protein operons. The nucleotide sequences of resistant and susceptible isolates were compared, and a point mutation (thymine to guanine) that causes an Ile52-Ser substitution in ribosomal protein L16 was identified. The role of this mutation in decreasing susceptibility to evernimicin was confirmed by direct transformation of the altered L16 gene. The presence of the L16 mutation in the resistant strain suggests that evernimicin is an inhibitor of protein synthesis. This was confirmed by inhibition studies using radiolabeled substrates, which showed that the addition of evernimicin at sub-MIC levels resulted in a rapid decrease in the incorporation of radiolabeled isoleucine in a susceptible isolate (SP#3) but was much less effective against SP#5. The incorporation of isoleucine showed a linear response to the dose level of evernimicin. The incorporation of other classes of labeled substrates was unaffected or much delayed, indicating that these were secondary effects.
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3

McNicholas, Paul M., Paul A. Mann, David J. Najarian, Lynn Miesel, Roberta S. Hare, and Todd A. Black. "Effects of Mutations in Ribosomal Protein L16 on Susceptibility and Accumulation of Evernimicin." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 79–83. http://dx.doi.org/10.1128/aac.45.1.79-83.2001.

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ABSTRACT Chemical mutagenesis of Staphylococcus aureus RN450 generated two strains that displayed a stable reduction (30- to 60-fold) in susceptibility to evernimicin. Cell-free translation reactions demonstrated that the resistance determinant was located in the ribosomal fraction. Compared to ribosomes isolated from a wild-type strain, ribosomes from the mutant strains displayed an 8- to 10-fold reduction in affinity for [14C]evernimicin. In contrast, the mutants displayed no alteration in either binding affinity or in vitro susceptibility to erythromycin. Exponential cultures of the mutant strains accumulated significantly less [14C]evernimicin than the wild-type strain, suggesting that accumulation is dependent on the high affinity that evernimicin displays for its binding site. Sequencing rplP (encodes ribosomal protein L16) in the mutant strains revealed a single base change in each strain, which resulted in a substitution of either cysteine or histidine for arginine at residue 51. Introduction of a multicopy plasmid carrying wild-type rplP into the mutant strains restored sensitivity to evernimicin, confirming that the alterations in rplP were responsible for the change in susceptibility. Overexpression of the mutant alleles in S. aureus RN450 had no effect on susceptibility to evernimicin, demonstrating that susceptibility is dominant over resistance.
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4

Souli, Maria, Claudie Thauvin-Eliopoulos, and George M. Eliopoulos. "In Vivo Activities of Evernimicin (SCH 27899) against Vancomycin-Susceptible and Vancomycin-Resistant Enterococci in Experimental Endocarditis." Antimicrobial Agents and Chemotherapy 44, no. 10 (October 1, 2000): 2733–39. http://dx.doi.org/10.1128/aac.44.10.2733-2739.2000.

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ABSTRACT To assess the potential efficacy of evernimicin (SCH 27899) against serious enterococcal infections, we used a rat model of aortic valve endocarditis established with either a vancomycin-susceptibleEnterococcus faecalis or a vancomycin-resistantEnterococcus faecium strain. Animals infected with either one of the test strains were assigned to receive no treatment (controls) or 5-day therapy with one of the following regimens: evernimicin 60-mg/kg of body weight intravenous (i.v.) bolus once daily, 60-mg/kg i.v. bolus twice daily (b.i.d.), 60 mg/kg/day i.v. by continuous infusion, or 120 mg/kg/day i.v. by continuous infusion. These regimens were compared with vancomycin at 150 mg/kg/day. In animals infected with E. faecalis, evernimicin at 120 mg/kg/day by continuous infusion significantly reduced bacterial counts in vegetations (final density, 5.75 ± 3.38 log10CFU/g) compared with controls (8.51 ± 1.11 log10CFU/g). In animals infected with 0.5 ml of an 8 × 107-CFU/ml inoculum of the vancomycin-resistant E. faecium, both 60-mg/kg bolus once a day and b.i.d. dose regimens of evernimicin were very effective (viable counts, 3.45 ± 1.44 and 3.81 ± 1.98 log10 CFU/g, respectively). Vancomycin was unexpectedly active against infections induced with that inoculum. In animals infected with a 109-CFU/ml inoculum of the vancomycin-resistant E. faecium, the evernimicin 60-mg/kg i.v. bolus b.i.d. reduced viable counts in vegetations compared with controls (6.27 ± 1.63 versus 8.34 ± 0.91 log10 CFU/g; P < 0.05), whereas vancomycin was ineffective. Although resistant colonies could be selected in vitro, we were not able to identify evernimicin-resistant clones from cardiac vegetations. An unexplained observation from these experiments was the great variability in final bacterial densities within cardiac vegetations from animals in each of the evernimicin treatment groups.
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5

Boucher, Helen W., Claudie Thauvin-Eliopoulos, David Loebenberg, and George M. Eliopoulos. "In Vivo Activity of Evernimicin (SCH 27899) against Methicillin-Resistant Staphylococcus aureus in Experimental Infective Endocarditis." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 208–11. http://dx.doi.org/10.1128/aac.45.1.208-211.2001.

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ABSTRACT Currently, there exist few satisfactory alternatives to vancomycin for therapy of serious methicillin-resistant Staphylococcus aureus (MRSA) infections. We employed a rat model of aortic valve endocarditis to assess the potential efficacy of evernimicin (SCH 27899) compared with vancomycin against infection with a strain susceptible to both agents (MICs of 0.25 and 0.50 μg/ml, respectively). Infected animals were assigned to one of three groups: controls (no treatment), evernimicin at 60 mg/kg of body weight by intravenous (i.v.) infusion once daily, or vancomycin at 150 mg/kg of body weight per day by continuous i.v. infusion. Therapy was administered for 5.5 days. At the start of therapy, colony counts in vegetations were 6.63 ± 0.44 log10 CFU/g. In both treatment groups, bacterial density within vegetations was significantly reduced in comparison with control animals that had not been treated. Final colony counts were as follows (mean ± standard deviation): controls, 10.12 ± 1.51 log10 CFU/g of vegetation; evernimicin, 7.22 ± 2.91 log10 CFU/g of vegetation; vancomycin, 5.65 ± 1.76 log10 CFU/g of vegetation. The difference between the evernimicin and vancomycin groups was not significant. These results confirmed the bacteriostatic activity of evernimicin in vivo in an experimental model of severe MRSA infection.
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6

Pavia, Charles S., Gary P. Wormser, John Nowakowski, and Anthony Cacciapuoti. "Efficacy of an Evernimicin (SCH27899) In Vitro and in an Animal Model of Lyme Disease." Antimicrobial Agents and Chemotherapy 45, no. 3 (March 1, 2001): 936–37. http://dx.doi.org/10.1128/aac.45.3.936-937.2001.

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ABSTRACT The MICs of evernimicin at which 90% of Borrelia burgdorferi patient isolates were inhibited ranged from 0.1 to 0.5 μg/ml. Evernimicin was as effective as ceftriaxone againstB. burgdorferi in a murine model of experimental Lyme disease. As assessed by culturing the urinary bladders of infected C3H mice, no live Borrelia isolates were recoverable following antibiotic treatment.
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7

Aarestrup, Frank Møller, and Paul M. McNicholas. "Incidence of High-Level Evernimicin Resistance in Enterococcus faecium among Food Animals and Humans." Antimicrobial Agents and Chemotherapy 46, no. 9 (September 2002): 3088–90. http://dx.doi.org/10.1128/aac.46.9.3088-3090.2002.

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ABSTRACT Six high-level evernimicin-resistant Enterococcus faecium isolates were identified among 304 avilamycin-resistant E. faecium isolates from animals and 404 stool samples from humans with diarrhea. All four animal isolates, and one of the human isolates, were able to transfer resistance to a susceptible E. faecium strain. The resulting transconjugants all tested positive for the presence of emtA, a gene encoding a methyltransferase previously linked with high-level evernimicin resistance. The four transconjugants derived from animal isolates all carried the same plasmid, while a differently sized plasmid was found in the isolate from humans. This study demonstrated a low incidence of high-level evernimicin resistance mediated by the emtA gene in different E. faecium isolates of animal and human origin.
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8

Zbaida, Shmuel, Joan Brieland, Philip Krieter, David Loebenberg, Gopal Krishna, Debra Horne, Xiaowen Lu, et al. "In Vitro Uptake of SCH 27899 (Evernimicin) by Rat Alveolar Macrophages." Antimicrobial Agents and Chemotherapy 45, no. 3 (March 1, 2001): 959–61. http://dx.doi.org/10.1128/aac.45.3.959-961.2001.

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ABSTRACT The in vitro uptake of [14C]evernimicin ([14C]SCH 27899) by primary cultures of rat alveolar macrophages and hepatocytes was determined. Both cell populations exhibited linear rates of uptake. However, the initial rate of drug uptake by alveolar macrophages was about threefold higher than that by hepatocytes. These findings demonstrate that [14C]evernimicin is taken up by rat alveolar macrophages, supporting the likelihood that the drug is able to reach sites of infection.
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9

Champney, W. Scott, and Craig L. Tober. "Evernimicin (SCH27899) Inhibits both Translation and 50S Ribosomal Subunit Formation in Staphylococcus aureusCells." Antimicrobial Agents and Chemotherapy 44, no. 6 (June 1, 2000): 1413–17. http://dx.doi.org/10.1128/aac.44.6.1413-1417.2000.

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ABSTRACT The effects of the everninomicin antibiotic evernimicin (SCH27899) on growing Staphylococcus aureus cells were investigated. Cellular growth rates and viable cell numbers decreased with increasing antibiotic concentrations. The rate of protein synthesis, measured as35S-amino acid incorporation, declined in parallel with the growth rate. Significantly, the formation of the 50S ribosomal subunit was inhibited in a dose-dependent fashion as well. 30S ribosomal subunit synthesis was not affected over the same concentration range. Evernimicin did not stimulate the breakdown of mature ribosomal subunits. Pulse-chase labeling experiments revealed a reduced rate of 50S subunit formation in drug-treated cells. Two erythromycin-resistant strains of S. aureus that carried the ermC gene were as sensitive as wild-type cells to antibiotic inhibition. In addition, two methicillin-resistant S. aureus organisms, one sensitive to erythromycin and one resistant to the macrolide, showed similar sensitivities to evernimicin. These results suggest a use for this novel antimicrobial agent against antibiotic-resistant bacterial infections.
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10

Adrian, Peter V., Cara Mendrick, David Loebenberg, Paul McNicholas, Karen J. Shaw, Keith P. Klugman, Roberta S. Hare, and Todd A. Black. "Evernimicin (SCH27899) Inhibits a Novel Ribosome Target Site: Analysis of 23S Ribosomal DNA Mutants." Antimicrobial Agents and Chemotherapy 44, no. 11 (November 1, 2000): 3101–6. http://dx.doi.org/10.1128/aac.44.11.3101-3106.2000.

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ABSTRACT Spontaneous mutants of susceptible clinical and laboratory isolates of Streptococcus pneumoniae exhibiting reduced susceptibility to evernimicin (SCH27899; MIC, 0.5 to 4.0 mg/liter) were selected on plates containing evernimicin. Four isolates that did not harbor mutations in rplP (which encodes ribosomal protein L16) were further analyzed. Whole chromosomal DNA or PCR products of the 23S ribosomal DNA (rDNA) operons from these mutants could be used to transform the susceptible S. pneumoniae strain R6 to resistance at frequencies of 10−5 and 10−4, respectively, rates 10- to 100-fold lower than that for a single-allele chromosomal marker. The transformants appeared slowly (48 to 72 h) on selective medium, and primary transformants passaged on nonselective medium produced single colonies that displayed heterogeneous susceptibilities to evernimicin. A single passage on selective medium of colonies derived from a single primary transformant homogenized the resistance phenotype. Sequence analysis of the 23S rDNA and rRNA from the resistant mutants revealed single, unique mutations in each isolate at the equivalent Escherichia coli positions 2469 (A → C), 2480 (C → T), 2535 (G → A), and 2536 (G → C). The mutations map within two different stems of the peptidyltransferase region of domain V. Because multiple copies of rDNA are present in the chromosome, gene conversion between mutant and wild-type 23S rDNA alleles may be necessary for stable resistance. Additionally, none of the characterized mutants showed cross-resistance to any of a spectrum of protein synthesis inhibitors, suggesting that the target site of evernimicin may be unique.
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11

Kofoed, Christine B., and Birte Vester. "Interaction of Avilamycin with Ribosomes and Resistance Caused by Mutations in 23S rRNA." Antimicrobial Agents and Chemotherapy 46, no. 11 (November 2002): 3339–42. http://dx.doi.org/10.1128/aac.46.11.3339-3342.2002.

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ABSTRACT The antibiotic growth promoter avilamycin inhibits protein synthesis by binding to bacterial ribosomes. Here the binding site is further characterized on Escherichia coli ribosomes. The drug interacts with domain V of 23S rRNA, giving a chemical footprint at nucleotides A2482 and A2534. Selection of avilamycin-resistant Halobacterium halobium cells revealed mutations in helix 89 of 23S rRNA. Furthermore, mutations in helices 89 and 91, which have previously been shown to confer resistance to evernimicin, give cross-resistance to avilamycin. These data place the binding site of avilamycin on 23S rRNA close to the elbow of A-site tRNA. It is inferred that avilamycin interacts with the ribosomes at the ribosomal A-site interfering with initiation factor IF2 and tRNA binding in a manner similar to evernimicin.
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12

Kenny, George E., and Frank D. Cartwright. "Susceptibilities of Mycoplasma hominis, M. pneumoniae, and Ureaplasma urealyticum to GAR-936, Dalfopristin, Dirithromycin, Evernimicin, Gatifloxacin, Linezolid, Moxifloxacin, Quinupristin-Dalfopristin, and Telithromycin Compared to Their Susceptibilities to Reference Macrolides, Tetracyclines, and Quinolones." Antimicrobial Agents and Chemotherapy 45, no. 9 (September 1, 2001): 2604–8. http://dx.doi.org/10.1128/aac.45.9.2604-2608.2001.

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ABSTRACT The susceptibilities of Mycoplasma hominis,Mycoplasma pneumoniae, and Ureaplasma urealyticum to eight new antimicrobial agents were determined by agar dilution.M. pneumoniae was susceptible to the new glycylcycline GAR-936 at 0.12 μg/ml and evernimicin at 4 μg/ml, but it was resistant to linezolid. It was most susceptible to dirithromycin, quinupristin-dalfopristin, telithromycin, reference macrolides, and josamycin. M. hominis was susceptible to linezolid, evernimicin, and GAR-936. It was resistant to macrolides and the ketolide telithromycin but susceptible to quinupristin-dalfopristin and josamycin. U. urealyticum was susceptible to evernimicin (8 to 16 μg/ml) and resistant to linezolid. It was less susceptible to GAR-936 (4.0 μg/ml) than to tetracycline (0.5 μg/ml). Telithromycin and quinupristin-dalfopristin were the most active agents against ureaplasmas (0.06 μg/ml). The new quinolone gatifloxacin was active against M. pneumoniae and M. hominis at 0.12 to 0.25 μg/ml and active against ureaplasmas at 1.0 μg/ml. The MICs of macrolides were markedly affected by pH, with an 8- to 32-fold increase in the susceptibility of M. pneumoniae as the pH increased from 6.9 to 7.8. A similar increase in susceptibility with increasing pH was also observed with ureaplasmas. Tetracyclines showed a fourfold increase of activity as the pH decreased 1 U, whereas GAR-936 showed a fourfold decrease in activity with a decrease in pH.
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13

Mann, Paul A., Liqun Xiong, Alexander S. Mankin, Andrew S. Chau, Cara A. Mendrick, David J. Najarian, Christina A. Cramer, et al. "EmtA, a rRNA methyltransferase conferring high-level evernimicin resistance." Molecular Microbiology 41, no. 6 (September 2001): 1349–56. http://dx.doi.org/10.1046/j.1365-2958.2001.02602.x.

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14

Drusano, G. L., S. L. Preston, C. Hardalo, R. Hare, C. Banfield, D. Andes, O. Vesga, and W. A. Craig. "Use of Preclinical Data for Selection of a Phase II/III Dose for Evernimicin and Identification of a Preclinical MIC Breakpoint." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 13–22. http://dx.doi.org/10.1128/aac.45.1.13-22.2001.

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ABSTRACT One of the most challenging issues in the design of phase II/III clinical trials of antimicrobial agents is dose selection. The choice is often based on preclinical data from pharmacokinetic (PK) studies with animals and healthy volunteers but is rarely linked directly to the target organisms except by the MIC, an in vitro measure of antimicrobial activity with many limitations. It is the thesis of this paper that rational dose-selection decisions can be made on the basis of the pharmacodynamics (PDs) of the test agent predicted by a mathematical model which uses four data sets: (i) the distribution of MICs for clinical isolates, (ii) the distribution of the values of the PK parameters for the test drug in the population, (iii) the PD target(s) developed from animal models of infection, and (iv) the protein binding characteristics of the test drug. In performing this study with the new anti-infective agent evernimicin, we collected a large number (n = 4,543) of recent clinical isolates of gram-positive pathogens (Streptococcus pneumoniae,Enterococcus faecalis and Enterococcus faecium, and Staphylococcus aureus) and determined the MICs using E-test methods (AB Biodisk, Stockholm, Sweden) for susceptibility to evernimicin. Population PK data were collected from healthy volunteers (n = 40) and patients with hypoalbuminemia (n = 12), and the data were analyzed by using NPEM III. PD targets were developed with a neutropenic murine thigh infection model with three target pathogens: S. pneumoniae (n = 5), E. faecalis(n = 2), and S. aureus (n= 4). Drug exposure or the ratio of the area under the concentration-time curve/MIC (AUC/MIC) was found to be the best predictor of microbiological efficacy. There were three possible microbiological results: stasis of the initial inoculum at 24 h (107 CFU), log killing (pathogen dependent, ranging from 1 to 3 log10), or 90% maximal killing effect (90%E max). The levels of protein binding in humans and mice were similar. The PK and PD of 6 and 9 mg of evernimicin per kg of body weight were compared; the population values for the model parameters and population covariance matrix were used to generate five Monte Carlo simulations with 200 subjects each. The fractional probability of attaining the three PD targets was calculated for each dose and for each of the three pathogens. All differences in the fractional probability of attaining the target AUC/MIC in this PD model were significant. For S. pneumoniae, the probability of attaining all three PD targets was high for both doses. For S. aureus and enterococci, there were increasing differences between the 6- and 9-mg/kg evernimicin doses for reaching the 2 log killing (S. aureus), 1 log killing (enterococci), or 90%E max AUC/MIC targets. This same approach may also be used to set preliminary in vitro MIC breakpoints.
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15

Zarazaga, Myriam, Carmen Tenorio, Rosa Del Campo, Fernanda Ruiz-Larrea, and Carmen Torres. "Mutations in Ribosomal Protein L16 and in 23S rRNA in Enterococcus Strains for Which Evernimicin MICs Differ." Antimicrobial Agents and Chemotherapy 46, no. 11 (November 2002): 3657–59. http://dx.doi.org/10.1128/aac.46.11.3657-3659.2002.

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ABSTRACT Mutations in ribosomal protein L16 and in 23S rRNA were investigated in 22 Enterococcus strains of different species and for which the MICs of evernimicin differ (MICs, 0.023 to 16 μg/ml). Amino acid changes (Arg56His, Ile52Thr, or Arg51His) in protein L16 were found in seven strains, and a nucleotide G2535A mutation in 23S rRNA was found in 1 strain among 13 for which the MICs are ≥1 μg/ml.
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16

Hamilton-Miller, J. M. T., S. Shah, and D. Loebenberg. "Susceptibility of pneumococci to evernimicin: effect of CO2 and different methodologies." Clinical Microbiology and Infection 7, no. 6 (June 2001): 339–40. http://dx.doi.org/10.1046/j.1198-743x.2001.00252.x.

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17

Aarestrup, Frank Møller, and Lars Bogø Jensen. "Presence of Variations in Ribosomal Protein L16 Corresponding to Susceptibility of Enterococci to Oligosaccharides (Avilamycin and Evernimicin)." Antimicrobial Agents and Chemotherapy 44, no. 12 (December 1, 2000): 3425–27. http://dx.doi.org/10.1128/aac.44.12.3425-3427.2000.

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ABSTRACT Fragments (414 bp) of the gene-encoding ribosomal protein L16 fromEnterococcus faecium and Enterococcus faecalisthat were resistant and susceptible to the oligosaccharide antibiotics avilamycin and evernimicin (SCH 27899) were sequenced and compared. The susceptible E. faecalis and E. faecium isolates had sequences that were similar to those of the type strains. All resistant E. faecalis isolates contained the same base pair variation [CGT (Arg-56) → CAT (His-56)]. The same variation and two additional variations [ATC (Ile-52) → ACC (Thr-52) and ATC (Ile-52) → AGC (Ser-52)] were found in the resistant E. faecium isolates. This study indicated that resistance to the oligosaccharides in enterococci is associated with variations in the ribosomal protein L16.
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18

Tanaka, K. "In vitro activity of an evernimicin derivative, SCH27899, against anaerobic bacteria and Propionibacterium acnes." Journal of Antimicrobial Chemotherapy 46, no. 3 (September 1, 2000): 465–69. http://dx.doi.org/10.1093/jac/46.3.465.

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19

Zhong, Ruyun, Abraham Hernandez, Kevin B. Alton, Narendra S. Kishnani, and James E. Patrick. "High-performance liquid chromatographic method for the quantification of unbound evernimicin in human plasma ultrafiltrate." Journal of Chromatography B 772, no. 1 (May 2002): 191–95. http://dx.doi.org/10.1016/s1570-0232(02)00084-3.

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20

Arenz, Stefan, Manuel F. Juette, Michael Graf, Fabian Nguyen, Paul Huter, Yury S. Polikanov, Scott C. Blanchard, and Daniel N. Wilson. "Structures of the orthosomycin antibiotics avilamycin and evernimicin in complex with the bacterial 70S ribosome." Proceedings of the National Academy of Sciences 113, no. 27 (June 21, 2016): 7527–32. http://dx.doi.org/10.1073/pnas.1604790113.

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The ribosome is one of the major targets for therapeutic antibiotics; however, the rise in multidrug resistance is a growing threat to the utility of our current arsenal. The orthosomycin antibiotics evernimicin (EVN) and avilamycin (AVI) target the ribosome and do not display cross-resistance with any other classes of antibiotics, suggesting that they bind to a unique site on the ribosome and may therefore represent an avenue for development of new antimicrobial agents. Here we present cryo-EM structures of EVN and AVI in complex with the Escherichia coli ribosome at 3.6- to 3.9-Å resolution. The structures reveal that EVN and AVI bind to a single site on the large subunit that is distinct from other known antibiotic binding sites on the ribosome. Both antibiotics adopt an extended conformation spanning the minor grooves of helices 89 and 91 of the 23S rRNA and interacting with arginine residues of ribosomal protein L16. This binding site overlaps with the elbow region of A-site bound tRNA. Consistent with this finding, single-molecule FRET (smFRET) experiments show that both antibiotics interfere with late steps in the accommodation process, wherein aminoacyl-tRNA enters the peptidyltransferase center of the large ribosomal subunit. These data provide a structural and mechanistic rationale for how these antibiotics inhibit the elongation phase of protein synthesis.
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21

Goering, R., C. E. Nord, R. Hare, and F. Sabatelli. "In vitro activity of evernimicin and selected antibiotics against methicillin-resistant staphylococci: a 24-country study." Clinical Microbiology and Infection 6, no. 10 (October 2000): 549–56. http://dx.doi.org/10.1046/j.1469-0691.2000.00167.x.

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22

Belanger, Aimee E., and Thomas R. Shryock. "Avilamycin did not play a role in the discontinuation of evernimicin as a clinical drug candidate." Journal of Mass Spectrometry 40, no. 8 (August 2005): 1109. http://dx.doi.org/10.1002/jms.889.

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23

Belova, L., T. Tenson, L. Xiong, P. M. McNicholas, and A. S. Mankin. "A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit." Proceedings of the National Academy of Sciences 98, no. 7 (March 20, 2001): 3726–31. http://dx.doi.org/10.1073/pnas.071527498.

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24

Hosted, T. J., T. X. Wang, D. C. Alexander, and A. C. Horan. "Characterization of the biosynthetic gene cluster for the oligosaccharide antibiotic, Evernimicin, in Micromonospora carbonacea var. africana ATCC39149." Journal of Industrial Microbiology and Biotechnology 27, no. 6 (December 1, 2001): 386–92. http://dx.doi.org/10.1038/sj.jim.7000189.

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25

Krupkin, Miri, Itai Wekselman, Donna Matzov, Zohar Eyal, Yael Diskin Posner, Haim Rozenberg, Ella Zimmerman, Anat Bashan, and Ada Yonath. "Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding." Proceedings of the National Academy of Sciences 113, no. 44 (October 19, 2016): E6796—E6805. http://dx.doi.org/10.1073/pnas.1614297113.

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Abstract:
Two structurally unique ribosomal antibiotics belonging to the orthosomycin family, avilamycin and evernimicin, possess activity against Enterococci, Staphylococci, and Streptococci, and other Gram-positive bacteria. Here, we describe the high-resolution crystal structures of the eubacterial large ribosomal subunit in complex with them. Their extended binding sites span the A-tRNA entrance corridor, thus inhibiting protein biosynthesis by blocking the binding site of the A-tRNA elbow, a mechanism not shared with other known antibiotics. Along with using the ribosomal components that bind and discriminate the A-tRNA—namely, ribosomal RNA (rRNA) helices H89, H91, and ribosomal proteins (rProtein) uL16—these structures revealed novel interactions with domain 2 of the CTC protein, a feature typical to various Gram-positive bacteria. Furthermore, analysis of these structures explained how single nucleotide mutations and methylations in helices H89 and H91 confer resistance to orthosomycins and revealed the sequence variations in 23S rRNA nucleotides alongside the difference in the lengths of the eukaryotic and prokaryotic α1 helix of protein uL16 that play a key role in the selectivity of those drugs. The accurate interpretation of the crystal structures that could be performed beyond that recently reported in cryo-EM models provide structural insights that may be useful for the design of novel pathogen-specific antibiotics, and for improving the potency of orthosomycins. Because both drugs are extensively metabolized in vivo, their environmental toxicity is very low, thus placing them at the frontline of drugs with reduced ecological hazards.
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Jones, R. N. "In vitro Gram-positive antimicrobial activity of evernimicin (SCH 27899), a novel oligosaccharide, compared with other antimicrobials: a multicentre international trial." Journal of Antimicrobial Chemotherapy 47, no. 1 (January 1, 2001): 15–25. http://dx.doi.org/10.1093/jac/47.1.15.

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27

"P:5/3 – Evernimicin." Clinical Microbiology and Infection 6 (May 2000): 83. http://dx.doi.org/10.1016/s1198-743x(15)30166-x.

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