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Published on: February 10, 2023
α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles
Anastasia D Gazi1, Michael Kokkinidis2,3, Vasiliki E Fadouloglou4
1Unit of Technology & Service Ultrastructural Bio-Imaging (UTechS UBI), Institut Pasteur, 75015 Paris, France.
Type III Secretion Systems (T3SSs) deliver bacterial proteins into host cells. This review details how Type III Secretion Effectors (T3SEs) utilize unique protein folds, particularly alpha-helices, to manipulate host functions.
Area of Science:
- Microbiology
- Molecular Biology
- Structural Biology
Background:
- Type III Secretion Systems (T3SSs) are complex molecular machines in Gram-negative bacteria.
- T3SSs translocate bacterial proteins, known as effectors (T3SEs), into eukaryotic host cells.
Purpose of the Study:
- To review the diverse protein folds of T3SEs.
- To highlight the structural and functional significance of alpha-helices and helical domains in T3SEs.
Main Methods:
- Literature review of T3SS and T3SE structure-function relationships.
- Analysis of T3SE protein folding and unfolding mechanisms for translocation.
Main Results:
- T3SEs possess unique folds enabling unfolding for passage through the T3SS channel and refolding for activity.
- Alpha-helices and helical domains are crucial for T3SE function and host cell manipulation.
- T3SEs mimic eukaryotic proteins to hijack cellular processes, impacting host metabolism and defense.
Conclusions:
- The structural adaptability of T3SEs, particularly their helical elements, is key to their function.
- Understanding T3SE folds provides insights into bacterial pathogenesis and host-pathogen interactions.
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