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Aminoglycosides are potent bactericidal agents that inhibit bacterial protein synthesis by binding to the 30S ribosomal subunit. They are often used in combination with either beta-lactam or glycopeptides, especially for the treatment of complicated staphylococcal infections, as these drugs act synergically [1]. The main mechanism of aminoglycoside resistance in staphylococci is drug inactivation by cellular aminoglycoside-modifying enzymes (AMEs), which are categorized into four classes depending on the modifications they induce: acetyltransferases (AACs), phosphotransferases (APHs), nucleotidyltransferases (ANTS), and adenyltransferases (AADs). Among staphylococci, the most common AME is 6′-N-acetyltransferase-2 ″-O-phosphotransferase [AAC (6′)-APH (2 ″)], encoded by the aac (6′)-Ie-aph (2 ″) gene inactivating gentamicin, kanamycin, tobramycin, neomycin, and amikacin. 4′-O …