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Published on: March 1, 2019
Structure and function of a genetically engineered mimic of a nonenveloped virus entry intermediate
Manidipa Banerjee1, Jeffrey A Speir, Maggie H Kwan
1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Journal of Virology
|February 19, 2010
Summary
Calcium ions are crucial for Flock House virus (FHV) capsid stability and infectivity. Blocking calcium binding exposes a viral peptide, impacting host cell entry and membrane disruption.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Divalent metal ions are integral to many icosahedral virus capsid structures.
- Flock House virus (FHV) serves as a model to study metal ion effects on virus biology.
Purpose of the Study:
- To investigate the role of calcium ions in FHV capsid stability and infectivity.
- To understand how metal ion binding influences virus-host interactions and entry mechanisms.
Main Methods:
- Site-directed mutagenesis of FHV calcium-binding sites.
- Analysis of capsid stability and infectivity.
- Conformational analysis of the gamma peptide under varying pH conditions.
Main Results:
- Mutations at calcium-binding sites destabilized the FHV capsid and significantly reduced infectivity.
- Capsid architecture remained unchanged, but gamma peptide exposure increased at neutral pH.
- Calcium binding is essential for pH-dependent control of gamma peptide exposure and membrane disruption.
Conclusions:
- Calcium ions are vital for maintaining FHV structural integrity and regulating viral peptide exposure.
- FHV calcium-binding mutants mimic an early endosomal entry intermediate.
- This reveals a novel mechanism for metal ion requirement in virus entry and infectivity.
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