Cutibacterium acnes 50S ribosomal subunit (C. acnes 50S subunit)

The Cutibacterium acnes 50S ribosomal subunit is a fundamental component of the protein synthesis machinery in the Gram-positive bacterium C. acnes, which is a key factor in the development of acne vulgaris (StatPearls, 2023). This large subunit is composed of 23S and 5S ribosomal RNA (rRNA) and approximately 33 ribosomal proteins, providing the structural framework for the peptidyl transferase center where peptide bond formation occurs (UniProt, 2024). It is the primary molecular target for several major classes of antibiotics used in dermatology, including macrolides (e.g., erythromycin) and lincosamides (e.g., clindamycin), which bind to the 23S rRNA to obstruct the ribosomal exit tunnel or the peptidyl transferase site (PubMed, 2021). By halting the production of bacterial proteins, these treatments effectively reduce C. acnes colonization and the subsequent release of pro-inflammatory enzymes and chemotactic factors (NIH, 2022). However, the clinical utility of targeting this subunit is increasingly compromised by the emergence of resistant strains harboring specific point mutations in the 23S rRNA gene or methyltransferase enzymes (Journal of Clinical Medicine, 2020). As a result, the 50S subunit remains a focal point for the development of novel antimicrobial scaffolds that can overcome established resistance patterns in skin infections.

Other names

Propionibacterium acnes 50S ribosomal subunit50S ribosomal subunit (Cutibacterium acnes)Large ribosomal subunit of C. acnesBacterial ribosome 50S subunit in Cutibacterium acnes

Inhibition of bacterial protein synthesis by binding to the 50S ribosomal subunit, specifically blocking the peptidyl transferase center or the exit tunnel, thereby preventing peptide chain elongation (StatPearls, 2023; PubMed, 2021).