Key result
K4058 and K2052 residues stabilize RNA duplex structure and modulate RV virion capsid conformation.
Why the study?
No anti-RV drugs are currently available, and understanding capsid-RNA interactions and the functional roles of positively charged capsid residues may contribute to antiviral drug development.
Population
RV-B14 mutant virions carrying K4058A or K2052A substitutions and parental virions
Comparison
Mutant virions carrying K4058A or K2052A substitutions vs parental RV-B14 virion
Design
Cryogenic electron microscopy structural study
Authors
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May inform structure-based antiviral design; leaves open functional validation and therapeutic relevance in vivo.
Positively charged capsid residues K4058 and K2052 in human rhinovirus stabilize RNA duplexes and restrict capsid flexibility, revealing two conformational states of the virion.
Martínez-Romero et al. (2026) studied Human rhinovirus. K4058A or K2052A substitutions vs. Parental RV-B14 virion was evaluated on Atomic structure and equilibrium conformation dynamics. K4058 and K2052 residues stabilize the RNA duplex structure and modulate capsid conformation, supporting the existence of basal and activated conformational states of the RV virion.
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