ATC Group: J01A Tetracyclines

Chlortetracycline is a tetracycline antibiotic isolated from Streptomyces aureofaciens. It has a role as an antiprotozoal drug, a fluorescent probe, a calcium ionophore and an antibacterial drug.

Tetracyclines have a broad spectrum of anti-microbial activity and act by interfering with bacterial protein synthesis. They are active against a large number of gram positive and gram negative pathogenic bacteria, including some which are resistant to penicillin.

Doxycycline is primarily bacteriostatic and is believed to exert its antimicrobial effect by the inhibition of protein synthesis.

Eravacycline is an antibacterial drug. Its mechanism of action involves the disruption of bacterial protein synthesis by binding to the 30S ribosomal subunit thus preventing the incorporation of amino acid residues into elongating peptide chains.

Minocycline is a semi-synthetic derivative of tetracycline. Minocycline inhibits protein synthesis in susceptible bacteria. In common with other tetracyclines it is primarily bacteriostatic and has a similar spectrum of activity to other tetracyclines.

Omadacycline is an antibacterial drug. It should be used only to treat or prevent infections that are proven or strongly suspected to be caused by susceptible bacteria.

Oxytetracycline is a broad spectrum tetracycline antibiotic with activity against a large number of gram positive and gram negative bacteria. The product acts by interfering with bacterial protein synthesis.

Sarecycline is a narrow-spectrum tetracycline-class antibiotic indicated for the treatment of inflammatory lesions of non-nodular moderate to severe acne vulgaris in patients 9 years of age and older.

Tetracyclines are taken up into sensitive bacterial cells by an active transport process. Once within the cell they bind reversibly to the 30S subunit of the ribosome, preventing the binding of aminoacyl transfer RNA and inhibiting protein synthesis and hence cell growth.

Tigecycline, a glycylcycline antibiotic, inhibits protein translation in bacteria by binding to the 30S ribosomal subunit and blocking entry of amino-acyl tRNA molecules into the A site of the ribosome. This prevents incorporation of amino acid residues into elongating peptide chains.