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| Title | Structural determinants of endopilus assembly, stability, and functional specificity in bacterial type II secretion. |
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| Journal, issue, pages | Structure, Vol. 34, Issue 10, Page 1324-11335.e5, Year 2026 |
| Publish date | Aug 20, 2026 |
Authors | Maylis Lejeune / Stefaniia Ivashchenko / Régine Dazzoni / Benjamin Bardiaux / Ravi R Sonani / Matthijn Vos / Theis Jacobsen / Edward H Egelman / Michael Nilges / Olivera Francetic / Vladimir E Shevchik / Nadia Izadi-Pruneyre / ![]() |
| PubMed Abstract | Gram-negative bacteria employ the type II secretion system (T2SS) to transport folded protein effectors via a periplasmic helical polymer called the endopilus, composed of one major and four minor ...Gram-negative bacteria employ the type II secretion system (T2SS) to transport folded protein effectors via a periplasmic helical polymer called the endopilus, composed of one major and four minor pilin subunits. Endopili resemble type IV pili but feature a conserved calcium-binding site stabilizing their major pilins. Endopilus polymerization is coupled to substrate translocation through a dedicated outer membrane channel. We compared T2SSs from plant and human pathogens, Dickeya dadantii and Klebsiella oxytoca, respectively. Despite different ecological niches and secreted effectors, their major pilins (OutG and PulG) share >77% sequence identity. Using NMR and cryo-EM, we solved structures of calcium-bound OutG monomer, as well as OutG and PulG endopili at 3.6 Å resolution. Combining structural, mutational, and biophysical analyses with in vivo assays, we identified key determinants of secretion specificity and endopilus stability. Our findings reveal how minor sequence variations in conserved nanomachines drive functional adaptation to diverse environments. |
External links | Structure / PubMed:42624105 |
| Methods | EM (helical sym.) / NMR (solution) |
| Resolution | 3.6 Å |
| Structure data | EMDB-75832, PDB-11me: EMDB-75833, PDB-11mf: ![]() PDB-29jd: |
| Chemicals | ![]() ChemComp-CA: |
| Source |
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Keywords | PROTEIN FIBRIL / Endopilus / T2SS / PulG / PROTEIN TRANSPORT / Dickeya dadantii T2SS / major pilin / pilus / secretion |
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dickeya dadantii (bacteria)
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