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Unique structural features of flaviviruses' capsid proteins: new insights on structure-function relationship
Thais C Neves-Martins1, Nathane C Mebus-Antunes1, Icaro P Caruso2
1Institute of Medical Biochemistry Leopoldo de Meis (IBqM), Federal University of Rio de Janeiro (UFRJ), 21941-590, Rio de Janeiro, RJ, Brazil.
Current Opinion in Virology
|March 15, 2021
Summary
Flaviviruses capsid proteins possess unique structural features, including quaternary contacts, a positive surface charge, and a flexible helix. These characteristics are crucial for understanding their role in viral structure and function.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- The Flaviviridae family includes significant human viral pathogens like Dengue and Zika viruses.
- Flavivirus genomes are RNA, packaged by a small, basic capsid protein forming homodimers.
Purpose of the Study:
- To review the structural properties of flavivirus capsid proteins.
- To discuss the relationship between these structural features and protein function.
Main Methods:
- Atomic-resolution structures of four flavivirus capsid proteins were determined.
- Methods included nuclear magnetic resonance (NMR) spectroscopy and X-ray diffraction.
Main Results:
- Flavivirus capsid proteins exhibit predominant quaternary contacts stabilizing the structure.
- A highly electropositive surface is a conserved feature across these proteins.
- A flexible alpha-helix (α1) was identified as a key structural element.
Conclusions:
- The identified structural features—quaternary contacts, electropositive surface, and flexible helix—are critical for flavivirus capsid protein function.
- Understanding these properties aids in comprehending flavivirus replication and pathogenesis.
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