The actin cytoskeleton and bacterial infection
This volume describes the mechanisms which bacteria have created to secure their survival, proliferation and dissemination by subverting the actin cytoskeleton of host cells. Bacteria have developed a veritable arsenal of toxins, effector proteins and virulence factors that allow them to modify the...
Saved in:
| Main Author: | |
|---|---|
| Format: | Book |
| Language: | English |
| Published: |
Springer
2020
|
| Subjects: | |
| Online Access: | http://repository.vnu.edu.vn/handle/VNU_123/90783 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Institution: | Vietnam National University, Hanoi |
| Language: | English |
| Summary: | This volume describes the mechanisms which bacteria have created to secure their survival, proliferation and dissemination by subverting the actin cytoskeleton of host cells. Bacteria have developed a veritable arsenal of toxins, effector proteins and virulence factors that allow them to modify the properties of the intracellular actin cytoskeleton for their own purposes. Bacterial factors either modify actin directly as the main component of this part of the cytoskeleton or functionally subvert regulatory or signalling proteins terminating at the actin cytoskeleton. In short, this volume provides an overview of the various tricks bacteria have evolved to ℓ́ℓact on actinℓ́ℓ in order to hijack this essential host cell component for their own needs. As such, it will be of interest to scientists from many fields, as well as clinicians whose work involves infectious diseases.Preface; Contents; 45 Actin: Structure, Function, Dynamics, and Interactions with Bacterial Toxins; Abstract; 1 Introduction; 2 Actin; 2.1 Actin Structure; 2.2 Binding Sites on Actin for Actin-Binding Proteins; 2.3 Filamentous (F- ) Actin; 2.4 Actin Dynamics: Polymerization Behaviour; 3 Interactions with Actin-Binding Proteins (ABPs); 3.1 G-actin-Sequestering Proteins; 3.2 F-actin-Nucleating Proteins and Their Nucleation-Promoting Factors (NPFs); 3.3 F-actin-Elongating Proteins; 3.4 F-actin-Capping Proteins; 3.5 F-actin-Bundling and Cross-linking Proteins; 3.6 F-actin-Stabilizing Proteins. |
|---|