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Updated: Jun 5, 2025
10:12
Construction of Cyclic Cell-Penetrating Peptides for Enhanced Penetration of Biological Barriers
Published on: September 19, 2022
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The universal Rhs shell structure accommodates various toxins inside and different functional decorations on the
1Bacterial Genetics and Physiology, Faculté des Sciences, Université Libre de Bruxelles (ULB), Gosselies, Belgium; WEL Research Institute, avenue Pasteur 6, 1300 Wavre, Belgium.
Structure (London, England : 1993)
|December 6, 2024
Summary
Researchers determined the crystal structures of Rhs proteins, revealing conserved core structures. This finding is significant despite variations in associated proteins and delivery mechanisms.
Area of Science:
- Structural biology
- Microbiology
- Protein structure analysis
Background:
- Rhs proteins are a diverse family involved in bacterial interactions.
- Their structural basis and relationship to secretion systems remain incompletely understood.
- Type VI secretion system (T6SS) components like PAAR and VgrG are crucial for protein delivery.
Purpose of the Study:
- To elucidate the three-dimensional structures of Rhs proteins.
- To investigate the structural relationship between Rhs proteins and T6SS components (PAAR, VgrG).
- To understand how structural variations influence Rhs protein function and delivery.
Main Methods:
- X-ray crystallography was employed to determine high-resolution protein structures.
- Genetic fusion techniques were used to link Rhs proteins with PAAR or VgrG.
Main Results:
- Crystal structures of Rhs proteins fused to PAAR or VgrG were obtained.
- Significant structural similarities were identified across the Rhs protein core.
- Diverse accessory domains ('decorations') and varying delivery modes were observed surrounding the conserved core.
Conclusions:
- Rhs proteins share a conserved structural core, suggesting a common evolutionary origin and fundamental function.
- Structural plasticity in surrounding domains allows for functional diversification and adaptation to different delivery systems.
- These findings provide a structural framework for understanding Rhs protein function in bacterial cell-cell interactions and virulence.
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