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TitleRumicidins are a family of mammalian host-defense peptides plugging the 70S ribosome exit tunnel.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 8925, Year 2024
Publish dateOct 16, 2024
AuthorsPavel V Panteleev / Eugene B Pichkur / Roman N Kruglikov / Alena Paleskava / Olga V Shulenina / Ilia A Bolosov / Ivan V Bogdanov / Victoria N Safronova / Sergey V Balandin / Valeriya I Marina / Tatiana I Kombarova / Olga V Korobova / Olga V Shamova / Alexander G Myasnikov / Alexander I Borzilov / Ilya A Osterman / Petr V Sergiev / Alexey A Bogdanov / Olga A Dontsova / Andrey L Konevega / Tatiana V Ovchinnikova /
PubMed AbstractThe antimicrobial resistance crisis along with challenges of antimicrobial discovery revealed the vital necessity to develop new antibiotics. Many of the animal proline-rich antimicrobial peptides ...The antimicrobial resistance crisis along with challenges of antimicrobial discovery revealed the vital necessity to develop new antibiotics. Many of the animal proline-rich antimicrobial peptides (PrAMPs) inhibit the process of bacterial translation. Genome projects allowed to identify immune-related genes encoding animal host defense peptides. Here, using genome mining approach, we discovered a family of proline-rich cathelicidins, named rumicidins. The genes encoding these peptides are widespread among ruminant mammals. Biochemical studies indicated that rumicidins effectively inhibited the elongation stage of bacterial translation. The cryo-EM structure of the Escherichia coli 70S ribosome in complex with one of the representatives of the family revealed that the binding site of rumicidins span the ribosomal A-site cleft and the nascent peptide exit tunnel interacting with its constriction point by the conservative Trp23-Phe24 dyad. Bacterial resistance to rumicidins is mediated by knockout of the SbmA transporter or modification of the MacAB-TolC efflux pump. A wide spectrum of antibacterial activity, a high efficacy in the animal infection model, and lack of adverse effects towards human cells in vitro make rumicidins promising molecular scaffolds for development of ribosome-targeting antibiotics.
External linksNat Commun / PubMed:39414793 / PubMed Central
MethodsEM (single particle)
Resolution1.95 Å
Structure data

46632

9d89

EMDB-46632, PDB-9d89:
E. coli 50S ribosomal subunit in complex with PrAMP rumicidin-2 (focused refinement)
Method: EM (single particle) / Resolution: 1.95 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-MS6:
(2S)-2-amino-4-(methylsulfanyl)butane-1-thiol

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • beatragus hunteri (mammal)
KeywordsRIBOSOME / Proline-rich antimicrobial peptides / PrAMP / Cryo-EM

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