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Highly Conserved Core Residues Define Old-World Alphaviruses and Trace Early Evolutionary Divergence
Wendy Carolina Piña-Ruiz1,2, Luis Rubén Jaime-Rocha1,2, Andrea Castorena-Robles1,3
1High-Resolution Section, Research Center for Health Sciences and Biomedicine, Autonomous University of San Luis Potosi, San Luis Potosi, Mexico.
Journal of Molecular Evolution
|July 27, 2026
Summary
Alphavirus capsid proteins form icosahedral structures. Conserved amino acids in Old-World alphaviruses suggest ancestral assembly, while New-World variants show divergence, impacting viral replication and virulence.
Area of Science:
- Virology
- Structural Biology
- Evolutionary Biology
Background:
- Alphaviruses are RNA viruses known for their distinct double-icosahedral particle structure.
- Capsid assembly, specifically the formation of a T=4 icosahedral nucleocapsid core, is a critical step in the alphavirus life cycle.
Purpose of the Study:
- To identify key amino acids controlling alphavirus capsomer formation and core organization.
- To investigate the evolutionary history of these amino acids and their impact on viral assembly.
Main Methods:
- Combined structural, evolutionary, and phylogenetic analyses.
- Identified conserved and divergent amino acid residues within alphavirus capsid proteins.
Main Results:
- A conserved network of residues involved in protein-protein and capsomer-capsomer interactions was found in Old-World alphaviruses.
- This interaction network diverges in New-World alphavirus lineages.
- Divergence in these interactions likely altered assembly efficiency and pathways, potentially affecting replication and pathogenicity.
Conclusions:
- The common ancestor of Old-World and New-World alphaviruses likely used assembly mechanisms similar to present-day Old-World viruses.
- Changes in capsid assembly interactions may represent an adaptive trade-off, balancing replication efficiency with viral persistence.
- Understanding these capsid dynamics offers new targets for antiviral strategies and vaccine development.
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