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TitleNa-V-ATPase inhibitor curbs VRE growth and unveils Na pathway structure.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 3, Page 450-458, Year 2025
Publish dateNov 21, 2024
AuthorsKano Suzuki / Yoshiyuki Goto / Akihiro Otomo / Kouki Shimizu / Shohei Abe / Katsuhiko Moriyama / Satoshi Yasuda / Yusuke Hashimoto / Jun Kurushima / Sho Mikuriya / Fabiana L Imai / Naruhiko Adachi / Masato Kawasaki / Yumi Sato / Satoshi Ogasawara / So Iwata / Toshiya Senda / Mitsunori Ikeguchi / Haruyoshi Tomita / Ryota Iino / Toshio Moriya / Takeshi Murata /
PubMed AbstractVancomycin-resistant Enterococcus faecium (VRE) is a major cause of nosocomial infections, particularly endocarditis and sepsis. With the diminishing effectiveness of antibiotics against VRE, new ...Vancomycin-resistant Enterococcus faecium (VRE) is a major cause of nosocomial infections, particularly endocarditis and sepsis. With the diminishing effectiveness of antibiotics against VRE, new antimicrobial agents are urgently needed. Our previous research demonstrated the crucial role of Na-transporting V-ATPase in Enterococcus hirae for growth under alkaline conditions. In this study, we identified a compound, V-161, from 70,600 compounds, which markedly inhibits E. hirae V-ATPase activity. V-161 not only inhibits VRE growth in alkaline conditions but also significantly suppresses VRE colonization in the mouse small intestine. Furthermore, we unveiled the high-resolution structure of the membrane V part due to V-161 binding. V-161 binds to the interface of the c-ring and a-subunit, constituting the Na transport pathway in the membrane, thereby halting its rotation. This structural insight presents potential avenues for developing therapeutic agents for VRE treatment and elucidates the Na transport pathway and mechanism.
External linksNat Struct Mol Biol / PubMed:39572733
MethodsEM (single particle)
Resolution2.2 Å
Structure data

37440

8wci

EMDB-37440, PDB-8wci:
Cryo-EM structure of the inhibitor-bound Vo complex from Enterococcus hirae
Method: EM (single particle) / Resolution: 2.2 Å

Chemicals

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-NA:
Unknown entry


ChemComp, No image

ChemComp-W3K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • enterococcus hirae atcc 9790 (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / V-ATPase / Na+-transporting / membrane protein / ATP hydrolyses / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex

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