23S ribosomal RNA of Helicobacter pylori (23S rRNA) (23S rRNA)

The 23S ribosomal RNA (23S rRNA) is a fundamental component of the 50S large ribosomal subunit in Helicobacter pylori, serving as the catalytic heart of the ribosome (Taylor et al., 1997, Antimicrobial Agents and Chemotherapy). It is responsible for the peptidyl transferase activity that facilitates the formation of peptide bonds during protein synthesis. This molecule is of significant clinical importance as it is the primary molecular target for macrolide antibiotics, most notably clarithromycin, which is a cornerstone of therapy for H. pylori eradication (Megraud, 2004, Gut). Macrolides exert their antibacterial effect by binding to the peptidyl transferase loop in domain V of the 23S rRNA, thereby physically blocking the elongation of the nascent polypeptide chain (Vianna et al., 2016, World Journal of Gastroenterology). Resistance to these antibiotics is frequently driven by specific point mutations within the 23S rRNA gene, such as A2142G and A2143G, which reduce drug binding affinity (Megraud, 2004, Gut). Consequently, monitoring the status of the 23S rRNA is vital for managing H. pylori-associated conditions, including chronic gastritis, peptic ulcers, and gastric cancer. The emergence of resistant strains globally has made the 23S rRNA a key focus for molecular diagnostic testing to guide personalized antibiotic treatment. Beyond its role as a drug target, the 23S rRNA is essential for the survival and virulence of the pathogen within the human stomach.

Other names

23S rRNArrn gene productLarge subunit ribosomal RNAPeptidyl transferase center

Inhibition of bacterial protein synthesis by binding to the 50S ribosomal subunit (specifically domain V of the 23S rRNA) and blocking the nascent peptide exit tunnel (Vianna et al., 2016, World Journal of Gastroenterology).