Macrolide, lincosamide and streptogramin

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

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... 

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... 

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. 

The erythromycin ribosomal methylase (erm) genes encode 23S ribosomal RNA methylases. This modification results in reduced binding of aU known macrolides, lincosamides, and streptogramin B to the ribosome (MLS resistance). Novel triazine-containing methyltransferase inhibitors that may reverse erm-mediated resistance are under development (46). 

Lina G, Quaglia A, Reverdy ME, Leclercq R, Vandenesch F, Etienne J. Distribution of genes encoding resistance to macrolides, lincosamides, and streptogramins among staphylococci. Antimicrob Agents Chemother 1999 43(5) 1062-6. 

Solubility and pAl, Values Representative of Some Macrolide, Lincosamide, and Streptogramin Type B Antibiotics ... 

Fig. 2. Chemical structures of macrolide, lincosamide, and streptogramin type B antibiotics. Mac-rolide antibiotics (M) EM, CAM, AZM, HMR 3647, ABT-773, LM A5, RKM, TL, and YM133. Lin-cosamide antibiotics (L) LCM and CLDM. Streptogramin type B antibiotic (S) mikamycin B.

Horinouchi, S., Byeon, W. H., and Weisblum, B. (1983). A complex attenuator regulates inducible resistance to macrolides, lincosamides, and streptogramin type B antibiotics in Streptococcus sanguis. J. Bacterial. 154, 1252-1262. 

Weisblum, B. (1985). Inducible resistance to macrolides, lincosamides and streptogramin type B antibiotics The resistance phenotype, its biological diversity, and structural elements that regulate expression—a review. J. Antimicrob. Chemother. 16 (Suppl. A), 63-90. 

Matsuoka, M. (2000). Study of macrolide, lincosamide, and. streptogramin B antibiotics resistance in Staphylococcus aureus. Yakugaku Zasshi 120, 374-386 (in Japanese). 

Bacterial resistance to macrolides results from alterations in ribosomal structure with loss of macrolide binding affinity. The structural alteration very often involves methy-lation of ribosomal RNA and is attributed to enzymatic activity expressed by plasmids. Cross-resistance between macrolides, lincosamides, and streptogramins occurs as a result of these drugs sharing a common binding site on the ribosome. 

Champney WS, Tober CL, Specific inhibition of 50S ribosomal subunit formation in Staphylococcus aureus cells by 16-membered macrolide, lincosamide, and streptogramin B antibiotics, Curr. Microbiol. 2000 41 126-135. 

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