Cytolethal Distending Toxin Subunit B: A Review of Structure-Function Relationship
Benoît J Pons1,2, Julien Vignard3, Gladys Mirey4
1Toxalim (Research Centre in Food Toxicology), Université de Toulouse, INRA, ENVT, INP-Purpan, UPS, 31300 Toulouse, France. benoit.pons@inra.fr.
Toxins
|October 17, 2019
Summary
Cytolethal Distending Toxin (CDT) is a bacterial toxin causing cell damage and death. Research explores the CdtB subunit's structure-function relationship to understand its toxic mechanisms.
Area of Science:
- Microbiology
- Molecular Biology
- Toxicology
Background:
- Cytolethal Distending Toxin (CDT) is a key virulence factor from Gram-negative bacteria.
- CDT contributes to persistent infections and diverse pathologies.
- CDT induces host cell distension, cell cycle arrest, and DNA damage.
Purpose of the Study:
- To review the established structure-function relationships of the CdtB subunit.
- To explore the hypothesized enzymatic activities of CdtB.
- To highlight the importance of studying CDT toxicity mechanisms in disease.
Main Methods:
- Sequence and 3D structure analyses of CDT.
- Mutation experiments targeting predicted key residues in CdtB.
- Review of existing experimental data on CdtB function.
Main Results:
- CdtB subunit is responsible for CDT's toxic effects.
- Structural similarities suggest CdtB may act as a nuclease or phosphatase.
- Mutation studies provide insights into CdtB's functional domains.
Conclusions:
- Understanding CdtB structure-function is crucial for elucidating CDT toxicity.
- Further research is needed to fully unravel CdtB's molecular mechanisms.
- Investigating CDT in pathological contexts is essential for therapeutic development.
More Related Videos
10:01Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
20.3K
14:29Visualization of Bacterial Toxin Induced Responses Using Live Cell Fluorescence Microscopy
Published on: October 1, 2012
12.4K
Related Concept Videos
01:57Protein Complexes with Interchangeable Parts
2.8K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.8K
01:29Cytoskeletal Proteins in Bacteria
4.1K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
4.1K
01:18Assembly of Cytoskeletal Filaments
27.0K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
27.0K
01:19Septins
2.2K
Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
2.2K
02:41Protein Complex Assembly
16.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.5K
01:19Mechanism of Conjugation
702
Bacterial conjugation is a mechanism of horizontal gene transfer that enables the exchange of genetic material between bacterial cells through direct contact. This process is facilitated by a donor cell carrying a conjugative plasmid, which encodes genes necessary for pilus formation, DNA replication, and transfer. The conjugative plasmid plays a central role in initiating and executing the transfer of genetic material.The tra region of the conjugative plasmid encodes proteins responsible for...
702