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TitleCryo-EM identifies F-ENA of Bacillus thuringiensis as a widespread family of endospore appendages across Firmicutes.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7652, Year 2025
Publish dateAug 16, 2025
AuthorsMike Sleutel / Adrià Sogues / Nani Van Gerven / Unni Lise Jonsmoen / Inge Van Molle / Marcus Fislage / Laurent Dirk Theunissen / Nathan F Bellis / Diana P Baquero / Edward H Egelman / Mart Krupovic / Fengbin Wang / Marina Aspholm / Han Remaut /
PubMed AbstractFor over 100 years, Bacillus thuringiensis (Bt) has been used as an agricultural biopesticide to control pests caused by insect species in the orders of Lepidoptera, Diptera, and Coleoptera. Under ...For over 100 years, Bacillus thuringiensis (Bt) has been used as an agricultural biopesticide to control pests caused by insect species in the orders of Lepidoptera, Diptera, and Coleoptera. Under nutrient starvation, Bt cells differentiate into spores and associated toxin crystals that can adopt biofilm-like aggregates. We reveal that such Bt spore/toxin biofilms are embedded in a fibrous extrasporal matrix, and using cryoID, we resolved the structure and molecular identity of an uncharacterized type of pili, referred to here as Fibrillar ENdospore Appendages or F-ENA. F-ENA are monomolecular protein filaments anchored to the exosporium and tipped with a flexible fibrillum. Phylogenetic and structural analyses reveal that F-ENA are conserved in Bacilli and Clostridia, featuring head-neck domains with β-barrel necks that interlock via N-terminal hook peptides. In Bacillus, two collagen-like proteins (F-Anchor and F-BclA), respectively, tether F-ENA and form the distal tip. Sedimentation assays suggest F-ENA promotes spore clustering via F-BclA contacts and/or filament bundling.
External linksNat Commun / PubMed:40818982 / PubMed Central
MethodsEM (helical sym.)
Resolution3.23 - 4.1 Å
Structure data

48780

9n0b

EMDB-48780, PDB-9n0b:
Cryo-EM of spore appendage from Anaerovoracaceae
Method: EM (helical sym.) / Resolution: 4.1 Å

52523

9hze

EMDB-52523, PDB-9hze:
CryoEM structure of F-ENA fibers on the spores of Bacillus thuringiensis serovar kurstaki
Method: EM (helical sym.) / Resolution: 3.23 Å

52650

9i65

EMDB-52650, PDB-9i65:
Recombinant F-ENA-2 fibers
Method: EM (helical sym.) / Resolution: 4.1 Å

Source
  • bacillota bacterium (bacteria)
  • bacillus thuringiensis serovar kurstaki (bacteria)
  • cohnella sp. ov330 (bacteria)
KeywordsPROTEIN FIBRIL / ENA / endospore appendage / protein fiber / helical / endospore appendage; ENA; helical; protein fiber; bacillus thuringiensis serovar kurstaki / spore appendage / helical filament / protein polymer

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