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Viral infection controlled by a calcium-dependent lipid-binding module in ALIX
Christin Bissig1, Marc Lenoir, Marie-Claire Velluz
1Biochemistry Department, University of Geneva, 30 quai Ernest Ansermet, 1211 Geneva 4, Switzerland.
Developmental Cell
|May 14, 2013
Summary
Lysobisphosphatidic acid (LBPA) recruits ALIX to late endosomes. This interaction, dependent on calcium and ALIX
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- ALIX and lysobisphosphatidic acid (LBPA) are involved in viral nucleocapsid release.
- The precise mechanism of their interaction and role in viral infection is not fully understood.
Purpose of the Study:
- To elucidate the mechanism by which LBPA interacts with ALIX.
- To determine the role of this interaction in viral infection and endosome association.
Main Methods:
- Utilized MODA algorithm to predict membrane-docking sites in ALIX.
- Investigated LBPA and calcium binding to the ALIX Bro1 domain.
- Assessed the necessity of LBPA and calcium binding for endosome association and viral infection.
Main Results:
- LBPA is recognized in an exposed site within the ALIX Bro1 domain.
- LBPA interaction requires a tightly bound structural calcium ion.
- The Bro1 domain's unique fold and hydrophobic residues confer LBPA selectivity.
- LBPA and calcium binding, along with ALIX ESCRT binding and dimerization, are essential for endosome association and infection.
Conclusions:
- LBPA recruits ALIX to late endosomes via the calcium-bound Bro1 domain.
- This recruitment triggers a conformational change in ALIX.
- ALIX mediates viral nucleocapsid delivery to the cytosol during infection.
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