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Journal articles on the topic 'Streptogramine'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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1

De Gaudio, A. R., and A. Di Filippo. "Quale Ruolo per le Streptogramine in Terapia Intensiva?" Journal of Chemotherapy 15, sup1 (August 2003): 17–22. http://dx.doi.org/10.1080/1120009x.2003.11782355.

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2

Seoane, Asunción, and Juan M. García Lobo. "Identification of a Streptogramin A Acetyltransferase Gene in the Chromosome of Yersinia enterocolitica." Antimicrobial Agents and Chemotherapy 44, no. 4 (April 1, 2000): 905–9. http://dx.doi.org/10.1128/aac.44.4.905-909.2000.

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ABSTRACT Streptogramins are polypeptide antibiotics inhibiting protein synthesis by the prokaryotic ribosome. Gram-positive organisms are susceptible to streptogramins, while most gram-negative bacteria are intrinsically resistant. We have found a genomic fragment from aYersinia enterocolitica isolate with an open reading frame coding for a polypeptide similar to the virginiamycin acetyltransferases found in various plasmids from gram-positive bacteria. The susceptible Escherichia coli strain DB10 was transformed to resistance to the type A streptogramins and to mixed (A + B) streptogramins upon introduction of a plasmid containing that gene. In addition, we showed streptogramin acetylating activity in vitro dependent on the presence of the Y. enterocolitica sat gene. Southern blot hybridization experiments showed that thesat gene was present in all the Y. enterocolitica isolates examined. These data together show that the gene in the Y. enterocolitica chromosome encoded an active streptogramin acetyltransferase. The deduced sequence of theY. enterocolitica Sat protein was close to those ofsat gene products found in gram-positive bacteria and cyanobacteria, suggesting a common evolutionary origin.

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3

Foik, Ilona P., Irina Tuszynska, Marcin Feder, Elzbieta Purta, Filip Stefaniak, and Janusz M. Bujnicki. "Novel inhibitors of the rRNA ErmC' methyltransferase to block resistance to macrolides, lincosamides, streptogramine B antibiotics." European Journal of Medicinal Chemistry 146 (February 2018): 60–67. http://dx.doi.org/10.1016/j.ejmech.2017.11.032.

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4

Noeske, Jonas, Jian Huang, Nelson B. Olivier, Robert A. Giacobbe, Mark Zambrowski, and Jamie H. D. Cate. "Synergy of Streptogramin Antibiotics Occurs Independently of Their Effects on Translation." Antimicrobial Agents and Chemotherapy 58, no. 9 (June 23, 2014): 5269–79. http://dx.doi.org/10.1128/aac.03389-14.

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ABSTRACTStreptogramin antibiotics are divided into types A and B, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A, dalfopristin; type B, quinupristin) and NXL 103 (type A, flopristin; type B, linopristin) with theEscherichia coli70S ribosome by X-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. The streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a nonhydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that the synergistic antimicrobial activity of streptogramins can occur independently of the effects of streptogramin on translation.

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5

Stogios, Peter J., Misty L. Kuhn, Elena Evdokimova, Patrice Courvalin, Wayne F. Anderson, and Alexei Savchenko. "Potential for Reduction of Streptogramin A Resistance Revealed by Structural Analysis of Acetyltransferase VatA." Antimicrobial Agents and Chemotherapy 58, no. 12 (September 15, 2014): 7083–92. http://dx.doi.org/10.1128/aac.03743-14.

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ABSTRACTCombinations of group A and B streptogramins (i.e., dalfopristin and quinupristin) are “last-resort” antibiotics for the treatment of infections caused by Gram-positive pathogens, including methicillin-resistantStaphylococcus aureusand vancomycin-resistantEnterococcus faecium. Resistance to streptogramins has arisen via multiple mechanisms, including the deactivation of the group A component by the large family of virginiamycinO-acetyltransferase (Vat) enzymes. Despite the structural elucidation performed for the VatD acetyltransferase, which provided a general molecular framework for activity, a detailed characterization of the essential catalytic and antibiotic substrate-binding determinants in Vat enzymes is still lacking. We have determined the crystal structure ofS. aureusVatA inapo, virginiamycin M1- and acetyl-coenzyme A (CoA)-bound forms and provide an extensive mutagenesis and functional analysis of the structural determinants required for catalysis and streptogramin A recognition. Based on an updated genomic survey across the Vat enzyme family, we identified key conserved residues critical for VatA activity that are not part of theO-acetylation catalytic apparatus. Exploiting such constraints of the Vat active site may lead to the development of streptogramin A compounds that evade inactivation by Vat enzymes while retaining binding to their ribosomal target.

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6

Dupuis, Michel, and Roland Leclercq. "Activity of a New Oral Streptogramin, XRP2868, against Gram-Positive Cocci Harboring Various Mechanisms of Resistance to Streptogramins." Antimicrobial Agents and Chemotherapy 50, no. 1 (January 2006): 237–42. http://dx.doi.org/10.1128/aac.50.1.237-242.2006.

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ABSTRACT The antibacterial activity of XRP2868, a new oral streptogramin composed of a combination of RPR132552 (streptogramin A) and RPR202868 (streptogramin B), was evaluated against a collection of clinical gram-positive isolates with characterized phenotypes and genotypes of streptogramin resistance. The effects of genes for resistance to streptogramin A or B on the activity of XRP2868 and its components were also tested by cloning these genes individually or in various combinations in gram-positive recipient strains susceptible to quinupristin-dalfopristin. The species tested included Staphylococcus aureus, coagulase-negative staphylococci, Enterococcus faecalis, Enterococcus faecium, Streptococcus pneumoniae, and other species of streptococci. XRP2868 was generally fourfold more potent than quinupristin-dalfopristin against S. aureus, E. faecium, and streptococci and had activity against E. faecalis (MICs = 0.25 to 1 μg/ml). XRP2868 appeared to be affected by the same mechanisms of resistance as those to quinupristin-dalfopristin. Nevertheless, the strong activity of factor A of the oral streptogramin enabled the combination to be very potent against streptogramin-susceptible staphylococci, streptococci, and E. faecium (MICs = 0.03 to 0.25 μg/ml) and to retain low MICs against the strains harboring a mechanism of resistance to factor A or factor B of the streptogramin. However, the combination of mechanisms of resistance to factors A and B caused an increase in the MICs of XRP2868, which reached 1 to 4 μg/ml. As with the other streptogramins, there was a reduction in the bactericidal effect of XRPR2868 when the staphylococcal strains acquired a constitutively expressed erm gene.

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7

Lina, Gerard, Alain Quaglia, Marie-Elisabeth Reverdy, Roland Leclercq, François Vandenesch, and Jerome Etienne. "Distribution of Genes Encoding Resistance to Macrolides, Lincosamides, and Streptogramins among Staphylococci." Antimicrobial Agents and Chemotherapy 43, no. 5 (May 1, 1999): 1062–66. http://dx.doi.org/10.1128/aac.43.5.1062.

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ABSTRACT The relative frequency of 10 determinants of resistance to macrolides, lincosamides, and streptogramins was investigated by PCR in a series of 294 macrolide-, lincosamide-, and/or streptogramin-resistant clinical isolates of Staphylococcus aureus and coagulase-negative staphylococci isolated in 1995 from 32 French hospitals. Resistance was mainly due to the presence ofermA or ermC genes, which were detected in 259 strains (88%), in particular those resistant to methicillin (78% of the strains). Macrolide resistance due to msrA was more prevalent in coagulase-negative staphylococci (14.6%) than inS. aureus (2.1%). Genes related tolinA/linA′ and conferring resistance to lincomycin were detected in one strain of S. aureus and seven strains of coagulase-negative staphylococci. Resistance to pristinamycin and quinupristin-dalfopristin was phenotypically detected in 10 strains ofS. aureus and in three strains of coagulase-negative staphylococci; it was always associated with resistance to type A streptogramins encoded by vat or vatB genes and occurred in association with erm genes. The vgagene conferring decreased susceptibility to type A streptogramins was present alone in three strains of coagulase-negative staphylococci and in combination with erm genes in 10 strains of coagulase-negative staphylococci. A combination ofvga-vgb-vat and ermA genes was found in a single strain of S. epidermidis.

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8

Haroche, Julien, Jeanine Allignet, and Névine El Solh. "Tn5406, a New Staphylococcal Transposon Conferring Resistance to Streptogramin A and Related Compounds Including Dalfopristin." Antimicrobial Agents and Chemotherapy 46, no. 8 (August 2002): 2337–43. http://dx.doi.org/10.1128/aac.46.8.2337-2343.2002.

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ABSTRACT We characterized a new transposon, Tn5406 (5,467 bp), in a clinical isolate of Staphylococcus aureus (BM3327). It carries a variant of vgaA, which encodes a putative ABC protein conferring resistance to streptogramin A but not to mixtures of streptogramins A and B. It also carries three putative genes, the products of which exhibit significant similarities (61 to 73% amino acid identity) to the three transposases of the staphylococcal transposon Tn554. Like Tn554, Tn5406 failed to generate target repeats. In BM3327, the single copy of Tn5406 was inserted into the chromosomal att554 site, which is the preferential insertion site of Tn554. In three other independent S. aureus clinical isolates, Tn5406 was either present as a single plasmid copy (BM3318), as two chromosomal copies (BM3252), or both in the chromosome and on a plasmid (BM3385). The Tn5406-carrying plasmids also contain two other genes, vgaB and vatB. The insertion sites of Tn5406 in BM3252 were studied: one copy was in att554, and one copy was in the additional SCCmec element. Amplification experiments revealed circular forms of Tn5406, indicating that this transposon might be active. To our knowledge, a transposon conferring resistance to streptogramin A and related compounds has not been previously described.

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9

Allignet, Jeanine, Nadia Liassine, and Névine El Solh. "Characterization of a Staphylococcal Plasmid Related to pUB110 and Carrying Two Novel Genes, vatC andvgbB, Encoding Resistance to Streptogramins A and B and Similar Antibiotics." Antimicrobial Agents and Chemotherapy 42, no. 7 (July 1, 1998): 1794–98. http://dx.doi.org/10.1128/aac.42.7.1794.

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ABSTRACT We isolated and sequenced a plasmid, named pIP1714 (4,978 bp), which specifies resistance to streptogramins A and B and the mixture of these compounds. pIP1714 was isolated from a Staphylococcus cohnii subsp. cohnii strain found in the environment of a hospital where pristinamycin was extensively used. Resistance to both compounds and related antibiotics is encoded by two novel, probably cotranscribed genes, (i) vatC, encoding a 212-amino-acid (aa) acetyltransferase that inactivates streptogramin A and that exhibits 58.2 to 69.8% aa identity with the Vat, VatB, and SatA proteins, and (ii) vgbB, encoding a 295-aa lactonase that inactivates streptogramin B and that shows 67% aa identity with the Vgb lactonase. pIP1714 includes a 2,985-bp fragment also found in two rolling-circle replication and mobilizable plasmids, pUB110 and pBC16, from gram-positive bacteria. In all three plasmids, the common fragment was delimited by two direct repeats of four nucleotides (GGGC) and included (i) putative genes closely related to repB, which encodes a replication protein, and topre(mob), which encodes a protein required for conjugative mobilization and site-specific recombination, and (ii) sequences very similar to the double- and single-strand origins (dso, ssoU ) and the recombination site, RSA. The antibiotic resistance genes repBand pre(mob) carried by each of these plasmids were found in the same transcriptional orientation.

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10

Pechère, Jean-Claude. "Streptogramins." Drugs 51, Supplement 1 (1996): 13–19. http://dx.doi.org/10.2165/00003495-199600511-00005.

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11

Malbruny, Brigitte, Annie Canu, Bülent Bozdogan, Bruno Fantin, Virginie Zarrouk, Sylvie Dutka-Malen, Celine Feger, and Roland Leclercq. "Resistance to Quinupristin-Dalfopristin Due to Mutation of L22 Ribosomal Protein in Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 46, no. 7 (July 2002): 2200–2207. http://dx.doi.org/10.1128/aac.46.7.2200-2207.2002.

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ABSTRACT The mechanism of resistance to the streptogramin antibiotics quinupristin and dalfopristin was studied in a Staphylococcus aureus clinical isolate selected under quinupristin-dalfopristin therapy, in four derivatives of S. aureus RN4220 selected in vitro, and in a mutant selected in a model of rabbit aortic endocarditis. For all strains the MICs of erythromycin, quinupristin, and quinupristin-dalfopristin were higher than those for the parental strains but the MICs of dalfopristin and lincomycin were similar. Portions of genes for domains II and V of 23S rRNA and the genes for ribosomal proteins L4 and L22 were amplified and sequenced. All mutants contained insertions or deletions in a protruding β hairpin that is part of the conserved C terminus of the L22 protein and that interacts with 23S rRNA. Susceptible S. aureus RN4220 was transformed with plasmid DNA encoding the L22 alteration, resulting in transformants that were erythromycin and quinupristin resistant. Synergistic ribosomal binding of streptogramins A and B, studied by analyzing the fluorescence kinetics of pristinamycin IA-ribosome complexes, was abolished in the mutant strain, providing an explanation for quinupristin-dalfopristin resistance.

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12

Barrière, JC, Dh Bouanchaud, Jf Desnottes, and Jm Paris. "Streptogramin analogues." Expert Opinion on Investigational Drugs 3, no. 2 (February 1994): 115–31. http://dx.doi.org/10.1517/13543784.3.2.115.

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13

Mukhtar, Tariq A., Kalinka P. Koteva, and Gerard D. Wright. "Chimeric Streptogramin-Tyrocidine Antibiotics that Overcome Streptogramin Resistance." Chemistry & Biology 12, no. 2 (February 2005): 229–35. http://dx.doi.org/10.1016/j.chembiol.2004.12.009.

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14

Daurel, C., and R. Leclercq. "Lincosamides et streptogramines." EMC - Maladies infectieuses 7, no. 3 (January 2010): 1–11. http://dx.doi.org/10.1016/s1166-8598(10)38394-3.

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15

Bonfiglio, Giovanni, and Pio Maria Furneri. "Novel streptogramin antibiotics." Expert Opinion on Investigational Drugs 10, no. 2 (February 2001): 185–98. http://dx.doi.org/10.1517/13543784.10.2.185.

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16

Kamimiya, S., and B. Weisblum. "Induction of ermSV by 16-membered-ring macrolide antibiotics." Antimicrobial Agents and Chemotherapy 41, no. 3 (March 1997): 530–34. http://dx.doi.org/10.1128/aac.41.3.530.

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The erm family of 23S rRNA adenine-N6-methyltransferases confers resistance to all macrolide-lincosamide-streptograminB (MLS) antibiotics, but not all MLS antibiotics induce synthesis of Erm methyltransferase with equal efficiency in a given organism. The induction efficiency of a test panel of MLS antibiotics was studied by using two translational attenuator-lac reporter gene fusion constructs, one based on ermSV from Streptomyces viridochromogenes NRRL 2860 and the other based on ermC from Staphylococcus aureus RN2442. Four types of responses which were correlated with the macrolide ring size were seen, as follows: group 1, both ermSV and ermC were induced by the 14-membered-ring macrolides erythromycin, lankamycin, and matromycin, as well as by the lincosamide celesticetin; group 2, neither ermSV nor ermC was induced by the 12-membered-ring macrolide methymycin or by the lincosamide lincomycin or the streptogramin type B antibiotic ostreogrycin B; group 3, ermSV was selectively induced over ermC by the 16-membered-ring macrolides carbomycin, chalcomycin, cirramycin, kitasamycin, maridomycin, and tylosin; and group 4, ermC was selectively induced over ermSV by the 14-membered-ring macrolide megalomicin. These data suggest that the leader peptide determines the specificity of induction by different classes of MLS antibiotics and that for a given attenuator, a major factor which determines whether a given macrolide induces resistance is its size.

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17

Novotna, G., and J. Janata. "A New Evolutionary Variant of the Streptogramin A Resistance Protein, Vga(A)LC, from Staphylococcus haemolyticus with Shifted Substrate Specificity towards Lincosamides." Antimicrobial Agents and Chemotherapy 50, no. 12 (October 2, 2006): 4070–76. http://dx.doi.org/10.1128/aac.00799-06.

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ABSTRACT We found a new variant of the streptogramin A resistance gene, vga(A)LC, in clinical isolates of Staphylococcus haemolyticus resistant to lincomycin and clindamycin but susceptible to erythromycin and in which no relevant lincosamide resistance gene was detected. The gene vga(A)LC, differing from the gene vga(A) at the protein level by seven amino acid substitutions, was present exclusively in S. haemolyticus strains resistant to both lincosamides and streptogramin A (LSA phenotype). Antibiotic resistance profiles of the ATP-binding cassette (ABC) proteins Vga(A)LC and Vga(A) in the antibiotic-susceptible host S. aureus RN4220 were compared. It was shown that Vga(A)LC conferred resistance to both lincosamides and streptogramin A, while Vga(A) conferred significant resistance to streptogramin A only. Detailed analysis of the seven amino acid substitutions, distinguishing the two related ABC proteins with different substrate specificities, identified the substrate-recognizing site: four clustered substitutions (L212S, G219V, A220T, and G226S) in the spacer between the two ATP-binding cassettes altered the substrate specificity and constituted the lincosamide-streptogramin A resistance phenotype. A transport experiment with radiolabeled lincomycin demonstrated that the mechanism of lincosamide resistance in S. haemolyticus was identical to that of the reported macrolide-streptogramin B resistance conferred by Msr(A).

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18

Bonfiglio, Giovanni, and Pio Maria Furneri. "Patents on streptogramin antibiotics." Expert Opinion on Therapeutic Patents 13, no. 5 (May 2003): 651–59. http://dx.doi.org/10.1517/13543776.13.5.651.

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19

Malbruny, Brigitte, Anja M. Werno, David R. Murdoch, Roland Leclercq, and Vincent Cattoir. "Cross-Resistance to Lincosamides, Streptogramins A, and Pleuromutilins Due to thelsa(C) Gene inStreptococcus agalactiaeUCN70." Antimicrobial Agents and Chemotherapy 55, no. 4 (January 18, 2011): 1470–74. http://dx.doi.org/10.1128/aac.01068-10.

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ABSTRACTStreptococcus agalactiaeUCN70, isolated from a vaginal swab obtained in New Zealand, is resistant to lincosamides and streptogramins A (LSAphenotype) and also to tiamulin (a pleuromutilin). By whole-genome sequencing, we identified a 5,224-bp chromosomal extra-element that comprised a 1,479-bp open reading frame coding for an ABC protein (492 amino acids) 45% identical to Lsa(A), a protein related to intrinsic LSAresistance inEnterococcus faecalis. Expression of this novel gene, namedlsa(C), inS. agalactiaeBM132 after cloning led to an increase in MICs of lincomycin (0.06 to 4 μg/ml), clindamycin (0.03 to 2 μg/ml), dalfopristin (2 to >32 μg/ml), and tiamulin (0.12 to 32 μg/ml), whereas no change in MICs of erythromycin (0.06 μg/ml), azithromycin (0.03 μg/ml), spiramycin (0.25 μg/ml), telithromycin (0.03 μg/ml), and quinupristin (8 μg/ml) was observed. The phenotype was renamed the LSAP phenotype on the basis of cross-resistance tolincosamides,streptograminsA, andpleuromutilins. This gene was also identified in similar genetic environments in 17 otherS. agalactiaeclinical isolates from New Zealand exhibiting the same LSAP phenotype, whereas it was absent in susceptibleS. agalactiaestrains. Interestingly, this extra-element was bracketed by a 7-bp duplication of a target site (ATTAGAA), suggesting that this structure was likely a mobile genetic element. In conclusion, we identified a novel gene,lsa(C), responsible for the acquired LSAP resistance phenotype inS. agalactiae. Dissection of the biochemical basis of resistance, as well as demonstration ofin vitromobilization oflsa(C), remains to be performed.

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20

Barry, A. L., P. C. Fuchs, and S. D. Brown. "Antipneumococcal Activities of a Ketolide (HMR 3647), a Streptogramin (Quinupristin-Dalfopristin), a Macrolide (Erythromycin), and a Lincosamide (Clindamycin)." Antimicrobial Agents and Chemotherapy 42, no. 4 (April 1, 1998): 945–46. http://dx.doi.org/10.1128/aac.42.4.945.

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ABSTRACT Four different compounds belonging to the macrolide-lincosamide-streptogramin B (MLSb) class of antimicrobial agents were tested against 611 Streptococcus pneumoniae strains. The ketolide (HMR 3647, previously RU66647) and the streptogramin (quinupristin-dalfopristin) were both active against pneumococci with high-level MLSb resistance (clindamycin-resistant strains) as well as those with low-level macrolide resistance (clindamycin-susceptible strains).

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21

OSBORNE, NEWTON G. "New Macrolides, Azalides, and Streptogramins." Journal of Gynecologic Surgery 8, no. 1 (January 1992): 53–54. http://dx.doi.org/10.1089/gyn.1992.8.53.

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22

Neu, Harold C. "Streptogramins—agents for the 1990s." Antimicrobic Newsletter 7, no. 9 (September 1990): 71–72. http://dx.doi.org/10.1016/0738-1751(90)90019-9.

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23

Murchison, Amanda. "Quinupristin–dalfopristin: a streptogramin antibiotic." Primary Care Update for OB/GYNS 9, no. 5 (September 2002): 176–77. http://dx.doi.org/10.1016/s1068-607x(02)00113-0.

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24

Bonfiglio, Giovanni, and Pio Maria Furneri. "Patents on streptogramin antibiotics therapeutics." Expert Opinion on Therapeutic Patents 13, no. 5 (2003): 651–59. http://dx.doi.org/10.1517/eotp.13.5.651.23026.

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25

OʼSullivan, Niamh, and Richard Wise. "Macrolide, lincosamide, and streptogramin antibiotics." Current Opinion in Infectious Diseases 3, no. 6 (December 1990): 743–50. http://dx.doi.org/10.1097/00001432-199012000-00002.

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26

Kieke, Amy L., Mark A. Borchardt, Burney A. Kieke, Susan K. Spencer, Mary F. Vandermause, Kirk E. Smith, Selina L. Jawahir, and Edward A. Belongia. "Use of Streptogramin Growth Promoters in Poultry and Isolation of Streptogramin‐ResistantEnterococcus faeciumfrom Humans." Journal of Infectious Diseases 194, no. 9 (November 2006): 1200–1208. http://dx.doi.org/10.1086/508189.

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27

Fitoussi, Frederic, Catherine Doit, Pierre Geslin, Naima Brahimi, and Edouard Bingen. "Mechanisms of Macrolide Resistance in Clinical Pneumococcal Isolates in France." Antimicrobial Agents and Chemotherapy 45, no. 2 (February 1, 2001): 636–38. http://dx.doi.org/10.1128/aac.45.2.636-638.2001.

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ABSTRACT The genetic basis of macrolide resistance was investigated in a collection of 48 genotypically unrelated clinical isolates ofStreptococcus pneumoniae obtained between 1987 and 1997 in France. All strains were resistant to erythromycin, clindamycin, and streptogramin B, exhibiting a macrolide-lincosamide-streptogramin B resistance phenotype, and harbored the erm(B) gene. None of the strains carried the mef(A) or erm(A) subclass erm(TR) gene.

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28

Green, Michael, Coburn Allen, John Bradley, Barry Dashefsky, Janet R. Gilsdorf, Mario J. Marcon, Gordon E. Schutze, et al. "In Vitro Activity of Telithromycin against Macrolide-Susceptible and Macrolide-Resistant Pharyngeal Isolates of Group A Streptococci in the United States." Antimicrobial Agents and Chemotherapy 49, no. 6 (June 2005): 2487–89. http://dx.doi.org/10.1128/aac.49.6.2487-2489.2005.

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ABSTRACT In vitro susceptibility testing of 2,797 group A streptococcus (GAS) isolates demonstrated that telithromycin was fully active against all macrolide-susceptible strains and among 80 of 115 macrolide-resistant GAS expressing the M phenotype. Telithromycin resistance was identified in 2 of 45 strains expressing the inducible macrolide-lincosamide-streptogramin B phenotype and four of nine isolates expressing the constitutive macrolide-lincosamide-streptogramin B resistance phenotype.

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29

Johnston, Nicole J., Joyce C. de Azavedo, James D. Kellner, and Donald E. Low. "Prevalence and Characterization of the Mechanisms of Macrolide, Lincosamide, and Streptogramin Resistance in Isolates ofStreptococcus pneumoniae." Antimicrobial Agents and Chemotherapy 42, no. 9 (September 1, 1998): 2425–26. http://dx.doi.org/10.1128/aac.42.9.2425.

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ABSTRACT Of a total of 147 erythromycin-resistant Streptococcus pneumoniae isolates, 64 (43.5%) were resistant to erythromycin, clindamycin, and streptogramin B (MLSBphenotype), 57 of which possessed the ermB gene. Eighty-two (55.8%) were resistant to erythromycin alone (M phenotype), 81 of which possessed the mefE gene. One was erythromycin and streptogramin B resistant but susceptible to clindamycin (MS phenotype) and possessed neither the erm gene nor the mefEgene.

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30

Osono, T., and H. Umezawa. "Pharmacokinetics of macrolides, lincosamides and streptogramins." Journal of Antimicrobial Chemotherapy 16, suppl A (January 1, 1985): 151–66. http://dx.doi.org/10.1093/jac/16.suppl_a.151.

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31

Barrière, J. C., and J. M. Paris. "RP 59500 and related semisynthetic streptogramins." Drugs of the Future 18, no. 9 (1993): 833. http://dx.doi.org/10.1358/dof.1993.018.09.228688.

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32

Mast, Yvonne, and Wolfgang Wohlleben. "Streptogramins – Two are better than one!" International Journal of Medical Microbiology 304, no. 1 (January 2014): 44–50. http://dx.doi.org/10.1016/j.ijmm.2013.08.008.

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33

Stratton, Charles W. "Quinupristin/dalfopristin: the first parenteral streptogramin." Antimicrobics and Infectious Diseases Newsletter 18, no. 6 (June 2000): 41–45. http://dx.doi.org/10.1016/s1069-417x(00)89007-x.

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34

Wang, Ge, and Diane E. Taylor. "Site-Specific Mutations in the 23S rRNA Gene ofHelicobacter pylori Confer Two Types of Resistance to Macrolide-Lincosamide-Streptogramin B Antibiotics." Antimicrobial Agents and Chemotherapy 42, no. 8 (August 1, 1998): 1952–58. http://dx.doi.org/10.1128/aac.42.8.1952.

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ABSTRACT Clarithromycin resistance in Helicobacter pylori is mainly due to A-to-G mutations within the peptidyltransferase region of the 23S rRNA. In the present study, cross-resistance to macrolide, lincosamide, and streptogramin B (MLS) antibiotics (MLS phenotypes) has been investigated for several clinical isolates of H. pylori. Two major types of MLS resistance were identified and correlated with specific point mutations in the 23S rRNA gene. The A2142G mutation was linked with high-level cross-resistance to all MLS antibiotics (type I), and the A2143G mutation gave rise to an intermediate level of resistance to clarithromycin and clindamycin but no resistance to streptogramin B (type II). In addition, streptogramin A and streptogramin B were demonstrated to have a synergistic effect on both MLS-sensitive and MLS-resistant H. pyloristrains. To further understand the mechanism of MLS resistance inH. pylori, we performed in vitro site-directed mutagenesis (substitution of G, C, or T for A at either position 2142 or 2143 of the 23S rRNA gene). The site-directed point mutations were introduced into a clarithromycin-susceptible strain, H. pylori UA802, by natural transformation followed by characterization of their effects on MLS resistance in an isogenic background. Strains with A-to-G and A-to-C mutations at the same position within the 23S rRNA gene had similar levels of clarithromycin resistance, and this level of resistance was higher than that for strains with the A-to-T mutation. Mutations at position 2142 conferred a higher level of clarithromycin resistance than mutations at position 2143. All mutations at position 2142 conferred cross-resistance to all MLS antibiotics, which corresponds to the type I MLS phenotype, whereas mutations at position 2143 were associated with a type II MLS phenotype with no resistance to streptogramin B. To explain that A-to-G transitions were predominantly observed in clarithromycin-resistant clinical isolates, we propose a possible mechanism by which A-to-G mutations are preferentially produced in H. pylori.

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35

Jung, Young-Hee, Eun Shim Shin, Okgene Kim, Jung Sik Yoo, Kyeong Min Lee, Jae Il Yoo, Gyung Tae Chung, and Yeong Seon Lee. "Characterization of Two Newly Identified Genes, vgaD and vatG, Conferring Resistance to Streptogramin A in Enterococcus faecium." Antimicrobial Agents and Chemotherapy 54, no. 11 (August 16, 2010): 4744–49. http://dx.doi.org/10.1128/aac.00798-09.

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ABSTRACT We characterized two new streptogramin A resistance genes from quinupristin-dalfopristin-resistant Enterococcus faecium JS79, which was selected from 79 E. faecium isolates lacking known genes encoding streptogramin A acetyltransferase. A 5,650-bp fragment of HindIII-digested plasmid DNA from E. faecium JS79 was cloned and sequenced. The fragment contained two open reading frames carrying resistance genes related to streptogramin A, namely, genes for an acetyltransferase and an ATP efflux pump. The first open reading frame comprised 648 bp encoding 216 amino acids with a predicted left-handed parallel β-helix domain structure; this new gene was designated vatG. The second open reading frame consisted of 1,575 bp encoding 525 amino acids with two predicted ATPase binding cassette transporters comprised of Walker A, Walker B, and LSSG motifs; this gene was designated vgaD. vgaD is located 65 bp upstream from vatG, was detected together with vatG in 12 of 179 quinupristin-dalfopristin-resistant E. faecium isolates, and was located on the same plasmid. Also, the 5.6-kb HindIII-digested fragment which was observed in JS79 was detected in nine vgaD- and vatG-containing E. faecium isolates by Southern hybridization. Therefore, it was expected that these two genes were strongly correlated with each other and that they may be composed of a transposon. Importantly, vgaD is the first identified ABC transporter conferring resistance to streptogramin A in E. faecium. Pulsed-field gel electrophoresis patterns and sequence types of vgaD- and vatG-containing E. faecium isolates differed for isolates from humans and nonhumans.

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36

Chesneau, Olivier, Heidi Ligeret, Negin Hosan-Aghaie, Anne Morvan, and Elie Dassa. "Molecular Analysis of Resistance to Streptogramin A Compounds Conferred by the Vga Proteins of Staphylococci." Antimicrobial Agents and Chemotherapy 49, no. 3 (March 2005): 973–80. http://dx.doi.org/10.1128/aac.49.3.973-980.2005.

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ABSTRACT The Vga and Msr resistance determinants, encoded by mobile genetic elements in various staphylococcal strains, belong to a family of ATP-binding cassette (ABC) proteins whose functions and structures are ill defined. Their amino acid sequences are similar to those of proteins involved in the immunity of streptomycetes to the macrolide-lincosamide-streptogramin antibiotics that they produce. Sequence analysis of the genomes of the gram-positive bacteria with low G+C contents revealed that Lmo0919 from Listeria monocytogenes is more closely related to Vga variants than to Msr variants. In the present study we compared the antibiotic resistance profiles conferred by the Vga-like proteins in two staphylococcal hosts. It was shown that Vga(A), the Vga(A) variant [Vga(A)v], and Lmo0919 can confer resistance to lincosamides and streptogramin A compounds, while only Vga(B) is able to increase the level of resistance to pristinamycin, a mixture of streptogramin A and streptogramin B compounds. By using polyclonal antibodies, we found that the Vga(A) protein colocalized with the β subunit of the F1-F0 ATPase in the membrane fractions of staphylococcal cells. In order to identify functional units in these atypical ABC proteins, such as regions that might be involved in substrate specificity and/or membrane targeting, we analyzed the resistance phenotypes conferred by various plasmids carrying parts or modified versions of the vga(A) gene and we determined the subcellular localization of the gene products. Only polypeptides composed of two ABC domains were detected in the cell membranes. No region of drug specificity was identified. Resistance properties were dependent on the integrities of both Walker B motifs.

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37

Vannuffel, Pascal, and Carlo Cocito. "Mechanism of Action of Streptogramins and Macrolides." Drugs 51, Supplement 1 (1996): 20–30. http://dx.doi.org/10.2165/00003495-199600511-00006.

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38

Rubinstein, Ethan, and Nathan Keller. "Future Prospects and Therapeutic Potential of Streptogramins." Drugs 51, Supplement 1 (1996): 38–42. http://dx.doi.org/10.2165/00003495-199600511-00008.

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39

El Solh, Névine, and Jeanine Allignet. "Staphylococcal resistance to streptogramins and related antibiotics." Drug Resistance Updates 1, no. 3 (January 1998): 169–75. http://dx.doi.org/10.1016/s1368-7646(98)80036-8.

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40

Fierro, J. Fernando, Carmen Vilches, Carlos Hardisson, and Jose A. Salas. "Streptogramins-inactivating activity in three producer streptomycetes." FEMS Microbiology Letters 58, no. 2-3 (April 1989): 243–46. http://dx.doi.org/10.1111/j.1574-6968.1989.tb03052.x.

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41

Johnston, Nicole, Tariq Mukhtar, and Gerard Wright. "Streptogramin Antibiotics: Mode of Action and Resistance." Current Drug Targets 3, no. 4 (August 1, 2002): 335–44. http://dx.doi.org/10.2174/1389450023347678.

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42

Werner, Guido, Ingo Klare, and Wolfgang Witte. "Molecular analysis of streptogramin resistance in enterococci." International Journal of Medical Microbiology 292, no. 2 (January 2002): 81–94. http://dx.doi.org/10.1078/1438-4221-00194.

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43

Kirst, Herbert A. "New macrolide, lincosaminide and streptogramin B antibiotics." Expert Opinion on Therapeutic Patents 20, no. 10 (July 21, 2010): 1343–57. http://dx.doi.org/10.1517/13543776.2010.505921.

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44

Tavares, Francis, Jon P. Lawson, and A. I. Meyers. "Total Synthesis of Streptogramin Antibiotics. (−)-Madumycin II." Journal of the American Chemical Society 118, no. 13 (January 1996): 3303–4. http://dx.doi.org/10.1021/ja954312r.

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45

BARRIERE, J. C., N. BERTHAUD, D. BEYER, S. DUTKA-MALEN, J. M. PARIS, and J. F. DESNOTTES. "ChemInform Abstract: Recent Developments in Streptogramin Research." ChemInform 29, no. 27 (June 21, 2010): no. http://dx.doi.org/10.1002/chin.199827347.

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46

Werner, Guido, Bianca Hildebrandt, Ingo Klare, and Wolfgang Witte. "Linkage of determinants for streptogramin A, macrolide-lincosamide-streptogramin B, and chloramphenicol resistance on a conjugative plasmid in Enterococcus faecium and dissemination of this cluster among streptogramin-resistant enterococci." International Journal of Medical Microbiology 290, no. 6 (October 2000): 543–48. http://dx.doi.org/10.1016/s1438-4221(00)80020-x.

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47

Madsen, Christian Toft, Lene Jakobsen, and Stephen Douthwaite. "Mycobacterium smegmatis Erm(38) Is a Reluctant Dimethyltransferase." Antimicrobial Agents and Chemotherapy 49, no. 9 (September 2005): 3803–9. http://dx.doi.org/10.1128/aac.49.9.3803-3809.2005.

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ABSTRACT The waxy cell walls of mycobacteria provide intrinsic tolerance to a broad range of antibiotics, and this effect is augmented by specific resistance determinants. The inducible determinant erm(38) in the nontuberculous species Mycobacterium smegmatis confers high resistance to lincosamides and some macrolides, without increasing resistance to streptogramin B antibiotics. This is an uncharacteristic resistance pattern falling between the type I and type II macrolide, lincosamide, and streptogramin B (MLSB) phenotypes that are conferred, respectively, by Erm monomethyltransferases and dimethyltransferases. Erm dimethyltransferases are typically found in pathogenic bacteria and confer resistance to all MLSB drugs by addition of two methyl groups to nucleotide A2058 in 23S rRNA. We show here by mass spectrometry analysis of the mycobacterial rRNA that Erm(38) is indeed an A2058-specific dimethyltransferase. The activity of Erm(38) is lethargic, however, and only a meager proportion of the rRNA molecules become dimethylated in M. smegmatis, while most of the rRNAs are either monomethylated or remain unmethylated. The methylation pattern produced by Erm(38) clarifies the phenotype of M. smegmatis, as it is adequate to confer resistance to lincosamides and 14-member ring macrolides such as erythromycin, but it is insufficient to raise the level of resistance to streptogramin B drugs above the already high intrinsic tolerance displayed by this species.

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48

Shrestha, Bidya, Winny Singh, V. Samuel Raj, Bharat Mani Pokhrel, and Tribhuban Mohan Mohapatra. "High Prevalence of Panton-Valentine Leukocidin (PVL) Genes in Nosocomial-AcquiredStaphylococcus aureusIsolated from Tertiary Care Hospitals in Nepal." BioMed Research International 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/790350.

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Methicillin-resistantStaphylococcus aureus(MRSA) carrying the important virulence determinant, Panton-Valentine leukocidin (PVL), is an emerging infectious pathogen associated with skin and soft tissue infections as well as life-threatening invasive diseases. In carrying out the first PVL prevalence study in Nepal, we screened 73 nosocomial isolates ofS. aureusfrom 2 tertiary care Nepali hospitals and obtained an overall PVL-positivity rate of 35.6% among the hospital isolates: 26.1% of MRSA and 51.9% of methicillin sensitiveS. aureus(MSSA) isolates were found to be positive for the PVL genes. PVL prevalence was not associated with a specific (i) infection site, (ii) age group, or (iii) hospital of origin. It was found to be positively associated with heterogeneous MRSA (73.3%) compared to homogeneous MRSA (3.2%) and MSSA (51.9%); negatively associated with multiresistant MRSA (22%) compared to nonmultiresistant MRSA (60%) and MSSA (51.9%); and positively associated with macrolide-streptogramin B resistance (93.8%) compared to macrolide-lincosamide-streptogramin B resistance (0%) and no-resistance (45.8%) types. Macrolide-streptogramin B resistance was confirmed by the presence ofmsr(A) gene. Restriction pattern analyses provided evidence to support the circulation of a limited number of clones of PVL-positive MRSA, arguing for the adaptability of these isolates to a hospital setting.

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Lomaestro, Ben M., and Laurie L. Briceland. "Streptogramins and their Potential Role in Geriatric Medicine." Drugs & Aging 13, no. 6 (1998): 443–65. http://dx.doi.org/10.2165/00002512-199813060-00004.

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50

Ridgway, Geoffrey L. "New Macrolides, Azalides and Streptogramins in Clinical Practice." Journal of Antimicrobial Chemotherapy 46, no. 2 (August 2000): 343. http://dx.doi.org/10.1093/jac/46.2.343-a.

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