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TitleTailoring Vibrio-Type Secretin Channel Protein GspD Toward "One-Take" Dual-Constriction Nanopore Sensors.
Journal, issue, pagesSmall, Vol. 21, Issue 49, Page e05878, Year 2025
Publish dateOct 19, 2025
AuthorsRonghui Liu / Qishun Feng / Kuo Zhang / Xin Dai / Jing Dai / Xinrong Guo / Wenfu Lin / Zhuofei Wang / Qiulan Wu / Yang Fu / Yi Li /
PubMed AbstractDual-constriction nanopores offer a second sensing region that enhances the interactions with analytes at the single-molecule level. However, existing biological nanopore complexes, i.e., CsgG-CsgF, ...Dual-constriction nanopores offer a second sensing region that enhances the interactions with analytes at the single-molecule level. However, existing biological nanopore complexes, i.e., CsgG-CsgF, are prone to dissociation upon high voltages, enforcing the development of robust "one-take" platforms. Here, Type II general secretin protein D from Vibrio cholerae (VcGspD) as a promising scaffold with dual-constrictions is proposed and engineered. Biochemical analysis reveals that truncation of the N0-N2 domains yields stable multimerization, with the N3 domain being essential. Cryo-electron microscopy (Cryo-EM) resolves the truncated VcGspD (N0-N2) as a 15-mer architecture, confirming its structural integrity and determining localizations of P471 and F472. By introducing a point mutation at position 346 (S346C) and conjugating cholesterol-maleimide, stable channel insertion in lipid bilayers is achieved. Electrophysiological characterization demonstrates a predominantly low-conductance dual-constriction architecture with constriction diameters of ≈2 nm both at the cap and central constriction sites. The F472A mutation, together with the mutations on both constrictions, gives rise to convergent open-channel current and confers high-voltage stability, thus enabling efficient sensing of both single-stranded DNA and polypeptides. The findings establish VcGspD as a promising platform toward dual-constriction nanopore sensing, paving the way for advancements in the development and engineering of secretin channels.
External linksSmall / PubMed:41110147
MethodsEM (single particle)
Resolution2.39 Å
Structure data

62181

9k8v

EMDB-62181, PDB-9k8v:
Cryo-EM structure of the Type II secretion system protein from Vibrio cholerae
Method: EM (single particle) / Resolution: 2.39 Å

Source
  • vibrio cholerae (bacteria)
KeywordsPROTEIN TRANSPORT / Secretion / GspD / nanopore sequencing

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