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Updated: Nov 1, 2025

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Structural interactions define assembly adapter function of a type II secretion system pseudopilin.

Cristian A Escobar¹, Badreddine Douzi², Geneviève Ball²

¹Department of Bacteriology, University of Wisconsin-Madison, Madison, WI, USA.

Structure (London, England : 1993)

|June 17, 2021

Summary

This summary is machine-generated.

Researchers elucidated the function of a key pseudopilin protein (XcpH) in the type II secretion system (T2SS). This protein acts as a crucial adapter, structurally integrating components of this essential bacterial virulence pathway.

Keywords:

PDB-Dev Pseudomonas aeruginosa chemical-shift perturbation cross-linking mass spectrometry pilin pseudopilin type II secretion type IV pili

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Area of Science:

Microbiology
Structural Biology
Biochemistry

Background:

Type IV filaments are widespread prokaryotic polymers.
The type II secretion system (T2SS) is a critical virulence pathway in many bacterial pathogens.
The precise molecular role of pseudopilin proteins within the T2SS architecture remained largely unknown.

Purpose of the Study:

To decipher the structural integration and function of the pseudopilin protein XcpH in the Xcp T2SS.
To understand how XcpH bridges different components of the type IV filament.

Main Methods:

Utilized multiple biophysical techniques to investigate protein structure and interactions.
Employed structural modeling to visualize the complete type IV filament.

Main Results:

Identified XcpH as the adapter protein connecting the initiating tip complex (XcpIJK) with the XcpG filament.
Demonstrated that each XcpH pseudopilin caps an XcpG protofilament, forming a pseudopilus.
Revealed that XcpH's N-terminal helix unwinding is essential for its adapter function, a property shared with XcpG.

Conclusions:

Provided a comprehensive, experimentally validated 3D structural model of a complete type IV filament.
Unveiled the critical adapter role of XcpH in T2SS assembly and function.
Highlighted conserved structural mechanisms, like helix unwinding, within the type IV filament superfamily.