Do human noroviruses also switch their shape?
National Institutes of Natural SciencesPeer-Reviewed Publication
A collaborative 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. Using recombinant VLPs and cryo-electron microscopy (cryo-EM) at near-atomic resolution, the researchers found that the P domain, the protruding region on the viral surface responsible for host interactions, exists in two different conformations: a resting state, in which the P domain lies close to the underlying shell (S) domain, and a rising state, in which the P domain is elevated above the shell. They further demonstrated that this structural transition is accompanied by a substantial reorganization of the interaction network between neighboring capsid proteins. The study was published in International Journal of Molecular Sciences on July 24, 2026.
- Journal
- International Journal of Molecular Sciences
- Funder
- National Research Foundation of Korea, Japan Agency for Medical Research and Development, Joint Research Program of the National Institute for Physiological Sciences, New Faculty Research Grant of Pusan National University 2023