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TitleDistinct immunity protein families mediate compartment-specific neutralization of a bacterial toxin.
Journal, issue, pagesCell Rep, Vol. 44, Issue 11, Page 116459, Year 2025
Publish dateNov 25, 2025
AuthorsFelicity Alcock / Yaping Yang / Justin Deme / Guillermina Casabona / Chriselle Mendonca / Fatima Ulhuq / Susan Lea / Tracy Palmer /
PubMed AbstractStaphylococcus aureus utilizes a type VII secretion system (T7SS) to secrete antibacterial toxins targeting competitor bacteria. EsxX is a T7SS substrate protein harboring an N-terminal LXG domain, ...Staphylococcus aureus utilizes a type VII secretion system (T7SS) to secrete antibacterial toxins targeting competitor bacteria. EsxX is a T7SS substrate protein harboring an N-terminal LXG domain, which is secreted by ST398 strains. We demonstrate that the EsxX C terminus is a membrane-depolarizing toxin with a glycine zipper motif. EsxX is profoundly toxic to bacteria, displaying toxicity from both cytoplasmic and extracellular compartments. A pair of polytopic membrane proteins, ExiCD, protects cells from intoxication by extracellular EsxX. By contrast, a distinct soluble heterodimer, ExiAB, neutralizes cytoplasmic EsxX by sequestration of its glycine zipper motif in a binding groove on ExiB. exiA-exiB co-occur with esxX, consistent with protection from self-toxicity prior to EsxX secretion. By contrast, ExiCD is encoded by both EsxX producers and in antitoxin islands of competitor strains that do not encode EsxX, consistent with providing immunity against the secreted form of the toxin.
External linksCell Rep / PubMed:41129315 / PubMed Central
MethodsEM (single particle)
Resolution6.0 Å
Structure data

EMDB-72654: EsxX-EsxA-EsxB low resolution volume
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • Staphylococcus aureus (bacteria)

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