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The 30S subunit is the target of antibiotics such as tetracycline and gentamicin. [11] These antibiotics specifically target the prokaryotic ribosomes, hence their usefulness in treating bacterial infections in eukaryotes. Tetracycline interacts with H27 in the small subunit as well as binding to the A-site in the large subunit. [11]
Inhibits bacterial protein synthesis by binding to the 50S subunit of the ribosome Fosfomycin: Monurol, Monuril: Acute cystitis in women: This antibiotic is not recommended for children and 75 and up of age: Inactivates enolpyruvyl transferase, thereby blocking cell wall synthesis Fusidic acid: Fucidin: Metronidazole: Flagyl
In ribosomal protection, a resistance gene encodes a protein that can have several effects, depending on what gene is transferred. [34] Twelve classes of ribosomal protection genes/proteins have been found. [35] Possible mechanisms of action of these protective proteins include: blocking tetracyclines from binding to the ribosome [36]
Cresomycin has been found to effective against bacteria that are resistant to multible antibiotics, including lincosamides, both in vitro and in vivo, being more potent than iboxamycin. [1] The antibiotic was found in time-kill studies to be bacteriostatic against S. aureus. In vitro safety experiments with human cells indicated low ...
Some antibiotics may also damage the mitochondrion, a bacteria-derived organelle found in eukaryotic, including human, cells. [52] Mitochondrial damage cause oxidative stress in cells and has been suggested as a mechanism for side effects from fluoroquinolones . [ 53 ]
Tetracycline inhibits protein synthesis by blocking the attachment of charged tRNA at the P site peptide chain. Tetracycline blocks the A-site so that a hydrogen bond is not formed between the amino acids. Tetracycline binds to the 30S and 50S subunit of microbial ribosomes. [3] Thus, it prevents the formation of a peptide chain. [25]
The structure of the kasugamycin-70S ribosome complex from Escherichia coli has been determined by X-ray crystallography at 3.5-A resolution. The drug binds within the messenger RNA channel of the 30S subunit between the universally conserved G926 and A794 nucleotides in 16S ribosomal RNA, which are sites of kasugamycin resistance.
A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Numerous mutations in domains of the 23S rRNA with Peptidyl transferase activity have resulted in antibiotic resistance.