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Related Experiment Video

Updated: Jun 17, 2026

Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System

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Four distinct structural domains in Clostridium difficile toxin B visualized using SAXS.

David Albesa-Jové¹, Thomas Bertrand, Elisabeth P Carpenter

¹Department of Life Sciences, Division of Cell and Molecular Biology, Centre for Molecular Microbiology and Infection, Flowers Building, Exhibition Road, Imperial College London, London SW7 2AZ, UK.

Journal of Molecular Biology

|January 15, 2010

Summary

We determined the low-resolution structure of Clostridium difficile toxin B (TcdB) using small-angle X-ray scattering. This revealed TcdB is monomeric and organized into four distinct structural domains, aiding understanding of its cell-disrupting function.

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Area of Science:

Microbiology
Structural Biology
Biochemistry

Background:

Clostridium difficile causes antibiotic-associated diarrhea and colitis.
Toxin A and Toxin B (TcdB) are key virulence factors of C. difficile.
Limited structural data of intact TcdB has hindered research.

Purpose of the Study:

To determine the low-resolution three-dimensional structure of native TcdB.
To elucidate the domain organization and shape of TcdB in solution.
To provide a structural framework for understanding TcdB intoxication mechanisms.

Main Methods:

Small-angle X-ray scattering (SAXS) was used to obtain an ab initio low-resolution structure of native TcdB.
SAXS data was combined with crystallographic and modeled structures of individual TcdB domains.
Analysis focused on TcdB's overall shape, dimensions, and domain arrangement in solution.

Main Results:

TcdB was found to be monomeric in solution.
TcdB exhibits a highly asymmetric shape with a maximum dimension of approximately 275 Å.
The structure revealed four distinct structural domains, including the glucosyltransferase, protease, repeat region, and a translocation domain.

Conclusions:

The study provides the first low-resolution structure of intact TcdB, revealing its monomeric nature and four-domain organization.
This structural information offers new insights into functional domain boundaries and interactions.
The findings provide a framework for understanding how TcdB undergoes conformational changes to facilitate cell intoxication.