Streptogramins

Resistance to Lincomycin. Resistance to lincomycin is developed slowly, and is usually caused by modification of 23S ribosomal RNA, which leads to co-resistance to macroHde, lincosaminide, and streptogramin B antibiotics (25). Inactivation of lincomycin by clinical isolates of strains of Staphjlococcus aureus and Staphjlococcus haemoljticus, though retention of sensitivity to macroHdes (see Antibiotics, macrolides) and streptogramins (see Antibiotics, peptides), has been found to be the consequence of the conversion of the antibiotic into its 3-(5 -adenylate) (26). [Pg.87]

Hydrolysis of macrolides by products of the ere genes detected in enterobacteria is only of scientific interest, while esterases VGB-A and VGB-B encoded by the vgb type genes mediate clinically relevant resistance in staphylococci to the B compound (quinupristin) of the streptogramin combination quinu-pristin-dalfopristin. [Pg.103]

Resistance to the A compound of streptogramins is mediated by products of the vat genes (virginiamycin acetyliransferase), of which at least five molecular classes are known (vatA-E). These genes are located on plasmids of Enterococcus faecium and frequently in combination with a gene encoding a streptogramin hydrolase (vga/vgb) in staphylococci. [Pg.104]

Leclercq R, Courvalin P (1991) Bacterial resistance to macrolide, lincosamide, and streptogramin antibiotics by target modification. Antimicrob Agents Chemother 35 1267-1272... [Pg.106]

Resistance to streptogramin type B antibiotics can be mediated in staphylococci and enterococci by plasmids carrying a vgb gene [2]. The Vgb enzyme is a lyase that linearizes the cyclic hexadepsipeptide by cleavage of the ester bond via an elimination reaction. [Pg.771]

Acetyl-CoA is also utilized as a cofactor to modify chloramphenicol by O-acetyltranferases (CATs). These enzymes have been found in many different bacterial genera and are usually plasmid encoded in clinical isolates. Furthermore, streptogramin type A antibiotics are acetylatedby Vat enzymes that occur on plasmids in staphylococci and enterococci. [Pg.771]

MsrA 14-, 15-Membered macrolides, streptogramin type B Staphylococci Plasmid... [Pg.773]

Macrolide, lincosamide and streptogramin B resistance (MLSb phenotype) can be linked to specific nucleotide changes within the 23 S rRNA of the large ribosomal subunit, mainly at position A2058 or neighbouring bases (E. coli numbering). This is the... [Pg.773]

Roberts MC, Sutcliffe J, Courvalin P et al (1999) Nomenclature for macrolide and macrolide-lincosamide-streptogramin B resistance determinats. Antimicrob Agents Chemother 43 2823-2830... [Pg.775]

Another example of macrocyclic RCM with a diene-ene was disclosed in 2000 by Meyers and coworkers in the first total synthesis of griseoviridin (223) [ 107]. Griseoviridin is a highly complex member of the family of streptogramin antibiotics, featuring a 23-membered unsaturated bis-lactam core incorporat-... [Pg.313]

A gene designated msrA has been identified in Staph, aureus which confers resistance to macrolides and streptogramins but not to lincosamides. Its function is unknown but the DNA sequence is homologous to genes coding for known efflux proteins. [Pg.191]

Horinouchi, S. and Weisblum, B. (1982) Nucleotide sequence and functional map of pE194, a plasmid that specifies inducible resistance to macrolide, lincosamide, and streptogramin type B antibodies. Journal of... [Pg.54]

Streptogramins peptide (XRP2868) — and cSSSIs protein syndiesis ... [Pg.73]

Vannnffel P, Cocito C. (1996) Mechanism of action of streptogramins and macrolides. Drugs 51 20-30. [Pg.180]

Johnston NJ, Mnkhtar TA, Wright GD. (2002) Streptogramin Antibiotics Mode of action and resistance. Curr Drug Targets 3 335-344. [Pg.180]

Mabe S, Champney WS. (2005) A comparison of a new oral streptogramin XRP 2868 with qninnpristindalfopristin against antibiotic-resistant strains of Haemophilus Influenzae, Staphylococcus Aureus, and Streptococcus Pneumoniae. Curr Microbiol 51 363-366. [Pg.181]

Macroiides Tetracyci ines Oxazoiidinones Aminogiycosides Streptogramins Lincosa mides... [Pg.353]

As a group, the protein biosynthesis inhibitors comprise the second largest class of antibiotics available for clinical use. Natural product classes of antibiotics that inhibit the protein biosynthesis are aminoglycosides, tetracyclines, chloramphenicol, macrolides, lincosamides, fusidic acid, streptogramins and mupirocin (Fig. 7). [Pg.362]

Macrolides, lincosamides and streptogramins are protein biosynthesis inhibitors that bind to 50S subunit of the ribosome and inhibit peptidyl tRNA translocation from the A-site to the P-site." Macrolides have a glycosylated 14-, 15- or 16-membered lactone ring structure and are produced by several species of Streptomyces. Lincosamide antibiotics were isolated initially from Streptomyces lincolnensis but later isolated from different species of Streptomcyces. Streptogramins were also isolated from Streptomycesgraminofaciens and subsequently from several different Streptomyces species. There are two structurally different streptogramins, A and B they are bacteriostatic individually and can be bactericidal when combined. [Pg.365]

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