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TitleBotulinum neurotoxins exploit host digestive proteases to boost their oral toxicity via activating OrfXs/P47.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 5, Page 864-875, Year 2025
Publish dateJan 21, 2025
AuthorsLinfeng Gao / Maria Barbara Nowakowska / Katja Selby / Adina Przykopanski / Baohua Chen / Maren Krüger / François Paul Douillard / Kwok-Ho Lam / Peng Chen / Ting Huang / Nigel Peter Minton / Martin Bernhard Dorner / Brigitte Gertrud Dorner / Andreas Rummel / Miia Lindström / Rongsheng Jin /
PubMed AbstractBotulinum neurotoxins (BoNTs) rank among the most potent toxins and many of them are produced by bacteria carrying the orfX gene cluster that also encodes four nontoxic proteins (OrfX1, OrfX2, OrfX3 ...Botulinum neurotoxins (BoNTs) rank among the most potent toxins and many of them are produced by bacteria carrying the orfX gene cluster that also encodes four nontoxic proteins (OrfX1, OrfX2, OrfX3 and P47). The orfX gene cluster is also found in the genomes of many non-BoNT-producing bacteria, often alongside genes encoding oral insecticidal toxins. However, the functions of these OrfXs and P47 remain elusive. Here, we demonstrate that the combined action of all four components (OrfXs and P47) drastically boosts the oral toxicity of BoNT in mice, following proteolytic activation by digestive proteases that oral toxins regularly confront. In particular, OrfX2 adopts a self-inhibiting state, engaging with BoNT through another clostridial protein, nontoxic non-hemagglutinin (NTNH), only after proteolytic activation. Cryo-electron microscopy studies unveil that two molecules of protease-activated OrfX2 simultaneously associate with NTNH, a binding mode crucial for boosting BoNT oral toxicity. Collectively, these studies offer novel insights into the physiological functions and regulatory mechanisms of OrfXs and P47 of BoNTs, shedding light on the pathogenesis of other bacterial toxins associated with homologous OrfXs and P47.
External linksNat Struct Mol Biol / PubMed:39838108 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 4.1 Å
Structure data

43784

9arj

EMDB-43784, PDB-9arj:
CryoEM structure of BoNT-NTNH-OrfX2 complex from Clostridium botulinum E1, major class
Method: EM (single particle) / Resolution: 3.4 Å

43785

9ark

EMDB-43785, PDB-9ark:
CryoEM structure of BoNT-NTNH-OrfX2 complex from Clostridium botulinum E1, minor class
Method: EM (single particle) / Resolution: 4.1 Å

43786

9arl

EMDB-43786, PDB-9arl:
CryoEM structure of BoNT-NTNH-OrfX2 complex from Clostridium botulinum strain A1-ST7B, major class
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • clostridium botulinum e1 str. 'bont e beluga' (bacteria)
  • clostridium botulinum a (bacteria)
  • clostridium botulinum a str. hall (bacteria)
KeywordsTOXIN / Botulinum neurotoxin / Progenitor toxin complex (PTC)

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