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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 protein interactions are conserved in Old-World lineages but diverge in New-World viruses. This divergence impacts viral assembly, replication, and pathogenicity, offering insights for antiviral strategies.
Area of Science:
- Virology
- Structural Biology
- Evolutionary Biology
Background:
- Alphaviruses are RNA viruses known for their distinctive double-icosahedral particle structure.
- Capsid assembly and core organization are crucial for alphavirus replication and pathogenesis.
Purpose of the Study:
- To identify key amino acids controlling alphavirus capsomer formation and core organization.
- To trace the evolutionary history of these amino acids and their impact on viral assembly.
Main Methods:
- Combined structural, evolutionary, and phylogenetic analyses.
- Investigated conserved and divergent amino acid residues in capsid proteins.
- Analyzed protein-protein and capsomer-capsomer interaction networks.
Main Results:
- Identified a conserved network of residues in Old-World alphaviruses governing capsid assembly.
- Observed divergence in these interaction networks in New-World alphavirus lineages.
- Proposed that altered assembly efficiency due to residue divergence affects replication and pathogenicity.
Conclusions:
- The evolutionary history of capsid protein interactions shapes alphavirus assembly pathways.
- Divergence in assembly mechanisms may explain differences in virulence between viral lineages.
- Findings provide a framework for developing novel antiviral strategies and vaccines.
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