Helicobacter pylori 23S ribosomal RNA domain V (23S rRNA domain V) (23S rRNA domain V)

The 23S ribosomal RNA (rRNA) domain V in Helicobacter pylori is a critical structural and functional component of the bacterial 50S ribosomal subunit. It forms the core of the peptidyl transferase center (PTC), which is responsible for catalyzing peptide bond formation during protein synthesis (Taylor et al., 1997, Antimicrob. Agents Chemother.). This domain is the primary therapeutic target for macrolide antibiotics, such as clarithromycin, which is a cornerstone of H. pylori eradication therapy (Megraud, 2004, Gut). Macrolides bind to specific nucleotides within domain V, effectively blocking the nascent peptide exit tunnel and halting translation (Vester & Douthwaite, 2001, Antimicrob. Agents Chemother.). Mutations within this domain, particularly at positions A2142 and A2143, are the leading cause of clinical resistance to clarithromycin (Versalovic et al., 1996, Antimicrob. Agents Chemother.). These mutations significantly impact the efficacy of treatment regimens for H. pylori-associated conditions like peptic ulcers and gastric cancer (Mégraud & Lehours, 2007, Clin. Microbiol. Rev.). Understanding the structural integrity of domain V is essential for monitoring antibiotic susceptibility and developing next-generation antimicrobial agents.

Other names

Peptidyl transferase center23S rRNALarge ribosomal subunit RNADomain V of 23S rRNA

Inhibition of bacterial protein synthesis by binding to the 23S rRNA and blocking the nascent peptide exit tunnel.