Aminoglycosides are among the most commonly used broad-spectrum antibiotics in the anti-infective armamentarium. Aminoglycosides work by binding to the bacterial 30S ribosomal subunit (some work by binding to the 50S subunit), inhibiting the translocation of the peptidyl-tRNA from the A-site to the P-site and also causing misreading of mRNA, leaving the bacterium unable to synthesize proteins vital to its growth. Different classes of aminoglycoside antibiotics bind to different sites on the rRNA, depending on the structural complementarity between the two.
The structural modifications of aminoglycosides result in a severe reduction of the ability of the modified antibiotic to bind to the target RNA. In bacteria, resistance to aminoglycosides is often due to enzymatic inactivation by acetyltransferase (Aac), nucleotidyltransferase (adenylyltransferases, Ant) and phosphotransferases (Aph).
Here is a list of aminoglycoside resistance types