The streptogramin antibiotics: update on their mechanism of action

Bibliography

• HIRAMATSU K, HANAKI H, INO T et al.: Methicillin- resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility. J. Antimicrob. Che-mother. (1997) 40:135–136.
   PubMed Web of Science ®Google Scholar
• HIRAMATSU K, ARITAKA N, HANAKI H et al.: Dissemina-tion in Japanese hospitals of strains of Staphylococcus aureus heterogeneously resistant to vancomycin. Lan-cet (1997) 350:1670–1673.
   PubMed Web of Science ®Google Scholar
• J. Antibact. Chemother. (1992) :30: (Supplement A). (Entire volume)
   Google Scholar
• VAZQUEZ D: The streptogramin family of antibiotics. In: Antibiotics Vol. III. Corcoran JN, Hahn FE (Eds.), Sprin-ger, Berlin, Heidelberg, New York (1975):521–534.
   Google Scholar
• MARTINELLI E, ZERILLI LF, VOLPE G, PAGANI HE, CAR-ELLI B: New antibiotics from Actinoplanes strains. Structure of A 17002 C. J. Antibiol (1979) 30:108–114.
   Google Scholar
• WEN-CHIH L, SEINER V, DEAN LD et al.: Production ofvernamycin by a Micromonospora. J. Antibiol (1981) 34:1515–1516.
   PubMed Web of Science ®Google Scholar
• PARIS JM, BARRIERE JC, SMITH C, BOST PE: The chemis-try of pristinamycins. In: Recent Progress in the Chemical Synthesis of Antibiotics. Lukacs G, Ohno M (Eds.), Springer Verlag, Berlin, Germany (1990):183–248.
   Google Scholar
• BARRIERE JC, BOUANCHAUD DH, DESNOTTES JF, PARIS JM: Streptogramin analogues. Exp. Opin. Invest. Drugs (1994) 3:115–131.
   Google Scholar
• NEU HC, CHIN NX, GU JW: The in vitro activity of new streptogramins, RP 59500, RP 57669 and RP54476, alone and in combination. J. Antimicrob. Chemother. (1992) 30 (Suppl. 483–94.
   Google Scholar
• BARRIERE JC, PARIS JM: RP 59500 and related semisyn-thetic streptogramins. Drugs Future (1993) 18:833–845.
   Google Scholar
• AMILS R, REIMIREZ L, SANZ JL et al.: Phylogeny of antibi-otic action. In: The Ribosome, Structure, Function & Evolu-tion. Hill WE et al. (Eds.), American Society for Microbiology, Washington DC, USA (1990645–654.
   Google Scholar
• YAMAGUCHI H, YOSHIDA Y, TANAKA N: Inhibition by mikamycins of polypeptide synthesis directed by na-tive messengers and synthetic polynucleotides. J. Bio-chem. (1966) 60:246–255.
   Google Scholar
• DI GIAMBATTISTA M, COCITO C: Action of ions and pHon the binding of virginiamycin S to ribosomes. Bio-chim. Biophys. Acta (1983) 757:92–100.
   PubMed Web of Science ®Google Scholar
• CLAYS K, DI GIAMBATTISTA M, PERSOONS A, ENGEL-BORGHS Y: A fluorescence lifetime study of virginia-mycin S using multifrequency phase fluorometry. Biochemistry (1991) 30:7271–7276.
   PubMed Web of Science ®Google Scholar
• CONTRERAS A, VAZQUEZ, D: Synergistic interaction of the streptogramins with the ribosome. Eur. J. Biochem. (1977) 74:549–551.
   PubMedGoogle Scholar
• MOUREAU P, ENGELBORGHS Y, DI GIAMBATTISTA M,COCITO C: Fluorescence stopped flow analysis of the interaction of virginiamycin components and eryth-romycin with bacterial ribosomes. J. Biol. Chem. (1983) 258:14233–14238.
   PubMedGoogle Scholar
• VANNUFFEL P, DI GIAMBATTISTA M, MORGAN EA, COCITO C: Identification of a single base change in ri-bosomal RNA leading to erythromycin resistance. Biol. Chem. (1992) 267:8377–8382.
   Web of Science ®Google Scholar
• BEYER D, VANNUFFEL P, PEPPER K: Quinupristin (RP57669): a new tool to investigate ribosome-group B streptogramin interactions. (In Press.)
   Google Scholar
• DI GIAMBATTISTA M, CHINALI G, COCITO C: The mo-lecular bases of the inhibitory activities of type A and type B synergimycins and related antibiotics on ribo-somes. j Antimicrob. Chemother. (1989) 24:485–507.
   PubMed Web of Science ®Google Scholar
• DI GIAMBATTISTA M, ENGELBORGHS Y, NYSSEN E, CLAYS K, COCITO C: Interaction between virginiamy-cin S and ribosomes is partly provided by a salt bridge with a Mg2+ ion. Biochemistry (1991) 30:7277–7282.
   PubMed Web of Science ®Google Scholar
• DI GIAMBATTISTA M, THIELEN APGM, MAASSEN JA, MOLLER W, COCITO C: Localization of virginiamycin S binding site on bacterial ribosomes by fluorescence energy transfer. Biochemistry (1986) 25:3540–3547.
   PubMed Web of Science ®Google Scholar
• DE BETHUNE MP, NIERHAUS KH: Characterisation of the binding of virginiamycin S to Escherichia coli ri-bosomes. Eur.J. Biochem. (1978) 86:187–191.
   PubMedGoogle Scholar
• FRANCESCHI FJ, NIERHAUS KH: Ribosomal proteins L15 and L16 are mere late assembly proteins of the large ri-bosomal subunit. Analysis of an Escherichia coli mu-tant lacking L15. J. Biol. Chem. (1990) 265:16676–16682.
   Google Scholar
• DI GIAMBATTISTA M, NYSSEN E, PECHER A, COCITO C: Affinity labeling of the virginiamycin S binding site on bacterial ribosome. Biochemistry (1990) 29:9203–9211.
   PubMed Web of Science ®Google Scholar
• BISCHOF 0, KRUFT V, WITTMANN-LIEBOLD B: Analysis of the puromycin binding site in the 70S ribosome of Escherichia coli at the peptide level. J. Biol. Chem. (1994) 269:18315–18319.
   PubMed Web of Science ®Google Scholar
• BISCHOF 0, URLAUB H, KRUFT V, WITTMANN-LIEBOLDB: Peptide environment of the peptidyl transferase center from Escherichia coli 70S ribosomes as deter-mined by thermoaffinity labeling with dihydrospira-mycin. J. Biol. Chem. (1995) 270:23060–23064.
   PubMed Web of Science ®Google Scholar
• DI GIAMBATTISTA M, ENGELBORGHS Y, NYSSEN E, COCITO C: Kinetics of binding of macrolides, linco-samides, and synergimycins to ribosomes. J. Biol. Chem. (1987) 262:8591–8597.
   PubMed Web of Science ®Google Scholar
• TERAOKA H, NIERHAUS KH: Proteins from Escherichiacoliribosomes involved in binding of erythromycin. J. Mol Biol. (1978) 126:185–193.
   PubMed Web of Science ®Google Scholar
• LOTTI M, DABBS ER, HASENBANK R, STOFFLER-MEILIKE M, STOFFLER G: Characterisation of a mutant from Escherichia coli lacking protein L15 and localisation of protein L15 by immuno-electron microscopy. Mol. Gen. Gent. (1983) 192:295–300.
   PubMedGoogle Scholar
• PARDO D, ROSSET R: Properties of ribosomes from erythromycin resistant mutants from Escherichia coli. Mol. Gen. Gent. (1977) 156:267–271.
   PubMedGoogle Scholar
• ARE VALO MA, TEJEDOR F, POLO F, BALETS JPG: Protein components of the erythromycin binding site in bacte-rial protein synthesis. J. Biol. Chem. (1988) 263:58–63.
   PubMed Web of Science ®Google Scholar
• WEISBLUM, B: Erythromycin resistance by ribosome modification. Antimicrob. Agents Chemother. (1995) 39:577–585.
   PubMed Web of Science ®Google Scholar
• LACROIX P, AUMERCIER M, CAPMAU ML, LE GOFFIC F:Studies on pristinamycin synergism in Staphylococ-cus aureus. J. Antibiot. (1986) 39:1314–1321.
   PubMed Web of Science ®Google Scholar
• FOURNET MP, DEFORGES L, ZINI R, BARRE J, TILLEMENTJP: Binding studies of macrolides, lincosamides and streptogramins to Streptococcus G group using [311]-e rythro my c in. Biochem. Pharmacol. (1987) 36:3495–3500.
   PubMed Web of Science ®Google Scholar
• SIGMUND CD, MORGAN EA: Erythromycin resistancedue to a mutation in a ribosomal RNA operon of Escherichia coli. Proc. Natl. Acad. Sci. USA (1982) 79:5602–5606.
   PubMed Web of Science ®Google Scholar
• VESTER B, GARRETT A: Plasmid-coded and site-directedmutation in Escherichia coli 23S RNA that confers re-sistance to erythromycin: implications for the mechanism of action of erythromycin. Biochimie (1987) 8:891–900.
   Web of Science ®Google Scholar
• PERNODET JL, FISH S, BLONDELET-ROUAULT MH, CUNDLIFFE E: The macrolide-lincosamide-streptogramin B resistance phenotypes characterized by using a specifically deleted, antibiotic-sensitive strain of Streptomyces lividans. Antimicrob. Agents Che-mother. (1996) 40:581–585.
   PubMed Web of Science ®Google Scholar
• VANNUFFEL P, DI GIAMBATTISTA M, COCITO C: The role of rRNA bases in the interaction of peptidyltransferase inhibitors with bacterial ribosomes. J. Biol. Chem. (1992) 267:16114–16120.
   PubMed Web of Science ®Google Scholar
• DOUTHWAITE S, AAGAARD C: Erythromycin binding is reduced in ribosomes with conformational alterations in the 23S rRNA peptidyl transferase. j Mol. Biol. (1993) 232:725–731.
   PubMed Web of Science ®Google Scholar
• MOAZED D, NOLLER HF: Chloramphenicol, erythromy-cin, carbomycin and vernamycin B protect overlap-ping sites in the peptidyltransferase region of 23S ribosomal RNA. Biochimie (1987) 69:879–884.
   PubMed Web of Science ®Google Scholar
• VANNUFFEL P, DI GIAMBATTISTA M, COCITO C: Chemi-cal probing of a virginiamycin M-promoted conforma-tional change of the peptidyltransferase domain. Nucl. Acids Res. (1994) 22:4449–4453.
   PubMed Web of Science ®Google Scholar
• RODRIGUEZ-FONSECA C, AMILS R, GARRETT RA: Fine structure of the peptidyl transferase center on 23S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J. Mol. Biol. (1995) 247:224–235.
   PubMed Web of Science ®Google Scholar
• CHINALI G, NYSSEN E, DI GIAMBATTISTA M, COCITO C:Inhibition of polypeptide synthesis in cell-free sys-tems by virginiamycin S and erythromycin. Evidence for a common mode of action of type B synergimycins and 14-membered macrolides. Biochim. Biophys. Acta (1988) 949:71–78.
   PubMed Web of Science ®Google Scholar
• CHINALI G, NYSSEN E, DI GIAMBATTISTA M, COCITO C: Action of erythromycin and virginiamycin S on polypeptide synthesis in cell-free systems. Biochim. Biophys. Acta (1988) 951:42–52.
   PubMed Web of Science ®Google Scholar
• MENNINGER JR, COLEMAN RA, TSAI LN: Erythromycin, lincosamides, peptidyl-tRNA dissociation, and ribo-somal editing. Mol. Genet. (1994) 243:225–233.
   PubMedGoogle Scholar
• MENNINGER JR: The accumulation of peptidyl-transfer RNA of isoaccepting transfer RNA families in Escheri-chia co/iwith temperature-sensitive peptidyl-transfer RNA hydrolase. J. Biol. Chem. (1978) 253:6808–6813.
   PubMed Web of Science ®Google Scholar
• AUMERCIER M, BOUHALLAB S, CAPMAU ML, LE GOFFIC F: RP 59500: a proposed mechanism for its bactericidal activity. J. Antimicrob. Chemother. (1992) 30 (Suppl A):9–14.
   Google Scholar
• CHITTUM HS, CHAMPNEY W: Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia colicells. Curr. Microbiol (1995) 30:273–279.
   PubMed Web of Science ®Google Scholar
• CHAMPNEY WS, BURDINE R: Macrolide antibiotics in-hibit 50S ribosomal subunit assembly in Bacillus sub-tilis and Staphylococcus aureus. Antimicrob. Agents Chemother. (1995) 39:2141-2144. © Ashley Publications Ltd. All rights reserved.Exp. Opin. Invest. Drugs (1998) 7(4)
   Google Scholar
• OBERBACJMER I: Streptogramine als modellsysteme fur den kationentransport durch membranen. Disserta-tion. Georg-August-Universitat, Goettingen (1979).
   Google Scholar
• MINH HOA DT, DINH KINH C, DANG TRIEU Q: Spectro-photometric titration method for the determination of thermodynamic parameters of metal complexing. Z. Chem. (1990) 30:224–225.
   Google Scholar
• AUMERCIER M, BOUHALLAB S, CAPMAU ML, LE GOFFIC F: Irreversible binding of pristinamycin IIA ( strepto-gramin A) to ribosomes explains its "lasting damage" effect. J. Antibiot. (1986) 39:1322–1328.
   PubMed Web of Science ®Google Scholar
• CHINALI G, VANLINDEN F, COCITO C: Action of virginia-mycin M on the stability of different ribosomal com-plexes to ultracentrifugation. Biochim. Biophys. Acta (1988) 950:67–74.
   PubMed Web of Science ®Google Scholar
• COCITO C, VOORMA HO, BOSCH L: Interference of vir-giniamycin M with the initiation and the elongation of peptide chains in cell-free systems. Biochim. Biophys. Acta (1974) 340:285–298.
   PubMed Web of Science ®Google Scholar
• CHINALI G, DI GIAMBATTISTA M, COCITO C: Ribosome protection by tRNA derivatives against inactivation by virginiamycin M: evidence for two types of interaction of tRNA with the donor site of peptidyl transferase. Biochemistry (1987) 26:1592–1597.
   PubMed Web of Science ®Google Scholar
• CHINALI G, MOUREAU P, COCITO C: The mechanism of action of virginiamycin M on the binding of aminoacyl-tRNA to ribosomes directed by elongation factor Tu. Eur. j Biochem. (1981) 118:577–583.
   PubMedGoogle Scholar
• CHINALI G, MOUREAU P, COCITO C: The action of vir-giniamycin M on the acceptor, donor, and catalytic sites of peptidyltransferase. J. Biol. Chem. (1984) 259:9563–9568.
   PubMed Web of Science ®Google Scholar
• ODOM OW, HARDESTY B: Use of 50 S-binding antibiot-ics to characterize the ribosomal site to which peptidyl-tRNA is bound. J. Biol. Chem. (1992) 267:19117–19122.
   PubMed Web of Science ®Google Scholar
• NIERHAUS KH: The allosteric three-site model for the ribosomal elongation cycle: features and future. Bio-chemistry (1990) 29:4997–5008.
   Google Scholar
• NIERHAUS KH, BEYER D, DABROWSKI M et al: The elon-gating ribosome: structural and functional aspects. Biochem. Cell Biol. (1995) 73, 1011–1021.
   PubMed Web of Science ®Google Scholar
• NOLLER HF, MOAZED D, STERN S et al.: Structure of rRNA and its functional interaction in translation. In: The Ribosome, Structure, Function & Evolution. Hill WE et al. (Eds.), American Society for Microbiology, Washington DC, USA (1990645–654.
   Google Scholar
• STEINER G, KUECHLER E, BARTA A: Photoaffinity label-ing at the peptidyl transferase center reveals two dif-ferent positions for the A- and P-sites in domain V of 23S rRNA. EMBO J (1988) 7:3949–3955.
   PubMed Web of Science ®Google Scholar
• BOUANCHAUD D: In vitro and in vivo synergic activity and fractional inhibitory concentration (FIC) of the components of a semisynthetic streptogramin, RP 59500. J. Antimicrob. Chemother. (1992) 30 (Suppl A):95–99.
   Google Scholar
• ELIOPOULOS GM, MOELLERING RC: Antimicrobial com-binations. In: Antibiotics in Laboratory Medicine, 4th Lorian V (Ed.), Wiliams & Wilkins, Baltimore, Maryland, USA (YEAR):330–396.
   Google Scholar
• SIEGRIST S, VELITCHKOVITCH S, LE GOFFIC F, MOREAU N: Mechanism of action of a 16-membered macrolide. Characteristics of dihydrosaramicin binding to Escherichia coli ribosome and the effects of some competitors. J. Antibiol (1982) 35:866–874.
   Google Scholar
• PARFAIT R, DE BETHUNE MP, COCITO C: A spectrofluo-rimetric study of the interaction between virginiamy-cin S and bacterial ribosomes. Mol Gen. Genet. (1978) 166:45–51.
   PubMedGoogle Scholar
• MOUREAU P, ENGELBORGHS Y, DI GIAMBATTISTA M,COCITO C: Fluorescence stopped flow analysis of the interaction of virginiamycin components and eryth-romycin with bacterial ribosomes. J. Biol. Chem. (1983) 258:14233–14238.
   PubMedGoogle Scholar
• PARFAIT R, COCITO C: Lasting damage to bacterial ribo-somes by reversibly bound virginiamycin M. Proc. Natl. Acad. ScL USA (1980) 77:5492–5496.
   PubMed Web of Science ®Google Scholar
• NYSSEN E, DI GIAMBATTISTA M, COCITO C: Analysis of the reversible binding of virginiamycin M to ribosome and particle functions after removal of the antibiotic. Biochim. Biophys. Acta (1989) 1009:39–46.
   PubMed Web of Science ®Google Scholar