Human norovirus capsid shifts between two shapes, cryo-EM reveals
A research team led by Kazuyoshi Murata has discovered that virus-like particles (VLPs) of human norovirus genotype GII.3 are not structurally rigid, but can adopt two distinct conformational states, similar to those previously reported for murine norovirus.
Research led by Kazuyoshi Murata has revealed that human norovirus genotype GII.3 is not a structurally rigid virus, but can exist in two distinct conformational states. Using recombinant virus-like particles (VLPs) and cryo-electron microscopy (cryo-EM) at near-atomic resolution, the researchers discovered that the protruding P domain on the viral surface exists in a resting state, close to the underlying shell domain, and a rising state, elevated by approximately 1 nm and rotated by about 55°.
This structural transition involves a substantial reorganization of the interaction network between neighboring capsid proteins, particularly the P1 subdomain. The study, published in the International Journal of Molecular Sciences, marks the first evidence that human norovirus capsid dynamics are similar to those observed in murine norovirus, suggesting that these conformational changes may play crucial roles in viral infectivity, receptor recognition, and immune evasion.
The findings could pave the way for developing next-generation vaccines and antiviral therapies targeting these dynamic structural changes.
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