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Published on: September 27, 2014
Mouse LSECtin as a model for a human Ebola virus receptor
Zoi Pipirou1, Alex S Powlesland, Imke Steffen
1Division of Molecular Biosciences, Department of Life Sciences, Imperial College, London, UK.
Glycobiology
|January 25, 2011
Summary
Mouse LSECtin, a C-type lectin, binds Ebola virus glycoprotein similarly to its human counterpart. This glycan-binding receptor
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- LSECtin is a C-type lectin and glycan-binding receptor found on sinusoidal endothelial cells.
- Understanding LSECtin's function is crucial for studying viral interactions and immune responses.
Purpose of the Study:
- To investigate the biochemical properties of mouse LSECtin.
- To compare the binding characteristics of mouse LSECtin with human LSECtin.
- To establish a model for studying human LSECtin using mouse LSECtin and knockout mice.
Main Methods:
- Bacterial expression of the C-type carbohydrate-recognition domain of mouse LSECtin.
- Solid-phase binding assays and glycan array analysis.
- Site-directed mutagenesis to identify key binding residues.
Main Results:
- Mouse LSECtin exhibits high-affinity binding to glycans with terminal GlcNAcβ1-2Man motifs, mimicking human LSECtin.
- Sequence differences near the binding site do not alter binding specificity.
- Both mouse and human LSECtin bind Ebola virus glycoprotein with equivalent affinities; GlcNAcβ1-2Man inhibits this interaction.
Conclusions:
- Mouse LSECtin's biochemical properties closely resemble those of human LSECtin.
- Mouse LSECtin and associated knockout models are suitable for studying human LSECtin's biological functions.
- The GlcNAcβ1-2Man disaccharide is a potential inhibitor of Ebola virus glycoprotein binding to LSECtin.
