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TitleA human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.
Journal, issue, pagesCell Host Microbe, Vol. 33, Issue 2, Page 200-217.e24, Year 2025
Publish dateFeb 12, 2025
AuthorsBentley Lim / Jinghua Xu / Igor H Wierzbicki / Carlos G Gonzalez / Zhe Chen / David J Gonzalez / Xiang Gao / Andrew L Goodman /
PubMed AbstractAntagonistic interactions play a key role in determining microbial community dynamics. Here, we report that one of the most widespread contact-dependent effectors in human gut microbiomes, Bte1, ...Antagonistic interactions play a key role in determining microbial community dynamics. Here, we report that one of the most widespread contact-dependent effectors in human gut microbiomes, Bte1, directly targets the PpiD-YfgM periplasmic chaperone complex in related microbes. Structural, biochemical, and genetic characterization of this interaction reveals that Bte1 reverses the activity of the chaperone complex, promoting substrate aggregation and toxicity. Using Bacteroides, we show that Bte1 is active in the mammalian gut, conferring a fitness advantage to expressing strains. Recipient cells targeted by Bte1 exhibit sensitivity to membrane-compromising conditions, and human gut microbes can use this effector to exploit pathogen-induced inflammation in the gut. Further, Bte1 allelic variation in gut metagenomes provides evidence for an arms race between Bte1-encoding and immunity-encoding strains in humans. Together, these studies demonstrate that human gut microbes alter the protein-folding capacity of neighboring cells and suggest strategies for manipulating community dynamics.
External linksCell Host Microbe / PubMed:39909037 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.4 - 3.2 Å
Structure data

EMDB-60115: Cryo-EM map of PpiD-YfgM-Bte1 complex
Method: EM (single particle) / Resolution: 3.2 Å

PDB-8zhs:
Structure of Mbp-Bte1 fusion protein
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-8zht:
Structure of PpiD-YfgM complex
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • Bacteroides (bacteria)
  • bacteroides thetaiotaomicron (bacteria)
  • Bacteroides fragilis (bacteria)
  • escherichia coli k-12 (bacteria)
  • bacteroides fragilis nctc 9343 (bacteria)
KeywordsANTITOXIN / antibacterial toxin / CHAPERONE / complex

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