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The 23S ribosomal RNA (23S rRNA) is a critical structural and functional component of the 50S large ribosomal subunit in Helicobacter pylori (NCBI, 2023). It forms the peptidyl transferase center (PTC), which is responsible for catalyzing the formation of peptide bonds during protein synthesis. This molecule is the primary pharmacological target for macrolide antibiotics, such as clarithromycin, which bind to the V domain of the 23S rRNA to obstruct the nascent peptide exit tunnel (StatPearls, 2023). Inhibition of this process prevents the elongation of polypeptide chains, leading to bacterial stasis or death. Resistance to these drugs frequently arises from specific point mutations in the 23S rRNA gene, notably at positions A2142 and A2143, which reduce drug binding affinity (Megraud, 2004; PubMed). Given H. pylori's role in chronic gastritis, peptic ulcers, and gastric cancer, the 23S rRNA remains a pivotal target for antimicrobial therapy and resistance monitoring.
Inhibition of bacterial protein synthesis by binding to the 50S ribosomal subunit and blocking the peptide exit tunnel or interfering with peptidyl transferase activity.
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