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A statistical model for activation of Factor C by binding to LPS aggregates
Y Miyagawa1, K Kikuchi2, M Tsuchiya3
1Faculty of Bioenvironmental Science, Kyoto Gakuen University, 1-1 Nanjo-Ohtani, Sogabe-cho, Kameoka, Kyoto, 621-8555, Japan.
European Biophysics Journal : EBJ
|October 21, 2019
Summary
Factor C activation by lipopolysaccharide (LPS) requires dimer formation, not single molecule binding. This dimeric activation model explains observed Factor C activity patterns with LPS aggregates.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Factor C is a key enzyme in the horseshoe crab hemolymph coagulation cascade.
- Lipopolysaccharide (LPS) is a potent activator of Factor C.
- Previous studies showed Factor C activity varies with LPS concentration.
Purpose of the Study:
- To determine the molecular mechanism of Factor C activation by LPS.
- To differentiate between monomeric and dimeric activation models.
- To model Factor C activity based on LPS concentration and aggregation.
Main Methods:
- Statistical modeling of published Factor C activity data.
- Comparison of monomeric and dimeric activation models against experimental data.
- Analysis of Factor C activity at varying LPS and Lipid A concentrations.
Main Results:
- Published data did not support a monomeric activation model for Factor C.
- A dimeric activation model accurately predicted Factor C activity, showing a bell-shaped curve.
- Maximum Factor C activity was observed at a specific LPS concentration.
Conclusions:
- Factor C activation is mediated by dimerization.
- Dimerization occurs through interactions with LPS aggregates.
- Smaller LPS aggregates are more effective activators than larger ones due to optimal Factor C dimerization.
