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A second SARS-CoV S2 glycoprotein internal membrane-active peptide. Biophysical characterization and membrane
Jaime Guillén1, Ana J Pérez-Berná, Miguel R Moreno
1Instituto de Biología Molecular y Celular, Campus de Elche, Universidad Miguel Hernández, E-03202 Elche-Alicante, Spain.
Biochemistry
|July 12, 2008
Summary
The SARS-CoV spike protein
Area of Science:
- Virology
- Biochemistry
- Molecular Biology
Background:
- The severe acute respiratory syndrome coronavirus (SARS-CoV) spike (S) glycoprotein mediates viral entry by fusing viral and target cell membranes.
- The S2 domain of the S protein contains potential fusion peptides crucial for this membrane fusion process.
Purpose of the Study:
- To investigate the interaction of the SARS-CoV S glycoprotein peptide (SARS IFP, segment 873-888) with model membranes.
- To determine the structural changes in the peptide and membranes upon binding.
Main Methods:
- Binding assays using model phospholipid membranes.
- Analysis of peptide-induced structural changes in both peptide and membranes.
Main Results:
- SARS IFP peptide binds to and interacts with phospholipid model membranes.
- The peptide exhibits higher affinity for negatively charged phospholipids compared to zwitterionic ones.
- SARS IFP binding decreases phospholipid acyl chain mobility and induces conformational changes depending on membrane composition.
Conclusions:
- These findings support the role of the SARS IFP peptide in SARS-CoV-mediated membrane fusion.
- The study suggests this peptide region may aid the fusion peptide and pretransmembrane segment in the fusion process.
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