Structural studies of ribosome from an anaerobic Bacteroidetes human pathogen Porphyromonas gingivalis

Nucleic Acids Res. 2025 May 22;53(10):gkaf458. doi: 10.1093/nar/gkaf458.

Abstract

Porphyromonas gingivalis, an anaerobic pathogen in chronic periodontitis, belongs to the Bacteroidota phylum and is associated with various virulence factors. Its antibiotic-resistant strains and its propensity to form biofilms pose a challenge to effective treatment. To explore therapeutic avenues, we studied the high-resolution cryogenic electron microscope structures of ribosomes from the wild-type P. gingivalis W83 and the macrolide-resistant mutant strain ermΔporN. The structural analysis revealed unique features primarily at the ribosome periphery. Together with the distinctive distribution of ribosomal RNA modifications, these findings offer insights into the therapeutical potential, such as creation of novel therapeutic compounds inhibiting the specific cellular functions of the P. gingivalis ribosomes. Moreover, the high-resolution structure of the ermΔporN ribosome in its complex with the approved antibiotic lefamulin suggests its repurposing against P. gingivalis. Furthermore, we provide a foundation for additional effective strategies to treat periodontitis and associated systemic diseases.

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Cryoelectron Microscopy
  • Drug Resistance, Bacterial / genetics
  • Humans
  • Porphyromonas gingivalis* / drug effects
  • Porphyromonas gingivalis* / genetics
  • Porphyromonas gingivalis* / pathogenicity
  • Porphyromonas gingivalis* / ultrastructure
  • RNA, Ribosomal / chemistry
  • RNA, Ribosomal / genetics
  • Ribosomes* / chemistry
  • Ribosomes* / drug effects
  • Ribosomes* / genetics
  • Ribosomes* / ultrastructure

Substances

  • Anti-Bacterial Agents
  • RNA, Ribosomal