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Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid
Dorothy D Majewski1, Mark Okon2, Florian Heinkel2
1Department of Biochemistry and Molecular Biology and the Center for Blood Research, University of British Columbia, Vancouver, BC, Canada.
Structure (London, England : 1993)
|September 3, 2020
Summary
This study reveals the structure of Salmonella enterica pilotin InvH and its interaction with secretin InvG. Understanding this interaction is key to how pilotins assemble the essential type III secretion system pore.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- The type III secretion system (T3SS) is crucial for Gram-negative pathogen virulence.
- Assembly of the T3SS outer membrane secretin pore requires pilotin lipoproteins.
Purpose of the Study:
- To elucidate the structural and biochemical basis of pilotin-secretin interaction.
- To characterize the Salmonella enterica pilotin InvH and its cognate secretin InvG.
Main Methods:
- X-ray crystallography for structural determination.
- Size-exclusion coupled multi-angle light scattering (SE-MALS).
- Small-angle X-ray scattering (SAXS).
- Nuclear Magnetic Resonance (NMR) spectroscopy.
Main Results:
- Salmonella enterica InvH is an α-helical, dimerized pilotin.
- InvH forms a stable homodimer in solution.
- The InvH-InvG complex forms a heterodimer with a hydrophobic interface.
Conclusions:
- Structural and biochemical data reveal the InvH-InvG interaction mechanism.
- This knowledge advances understanding of secretin pore assembly by pilotins.
- Insights into T3SS assembly may inform anti-virulence strategies.
