Rxivist logo

Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 73,470 bioRxiv papers from 319,827 authors.

Dynamic rotation of the protruding domain enhances the infectivity of norovirus

By Chihong Song, Reiko Takai-Todaka, Motohiro Miki, Kei Haga, Akira Fujimoto, Ryoka Ishiyama, Kazuki Oikawa, Masaru Yokoyama, Naoyuki Miyazaki, Kenji Iwasaki, Kosuke Murakami, Kazuhiko Katayama, Kazuyoshi Murata

Posted 17 Dec 2019
bioRxiv DOI: 10.1101/2019.12.16.878785

Norovirus is the major cause of epidemic nonbacterial gastroenteritis worldwide. Lack of structural information on infection and replication mechanisms hampers the development of effective vaccines and remedies. Here, using cryo-electron microscopy, we show that the capsid structure of murine noroviruses changes in response to aqueous conditions. By twisting the flexible hinge connecting two domains, the protruding (P) domain reversibly rises off the shell (S) domain in solutions of higher pH, but rests on the S domain in solutions of lower pH. Metal ions help to stabilize the latter conformation in this process. Furthermore, in the resting conformation, the cellular receptor CD300lf is readily accessible, and thus infection efficiency is significantly enhanced. Two P domain conformations were also found in the human norovirus GII.3 capsid. These results provide new insights into the infection mechanisms of the non-envelope viruses that function in dramatic environmental changes such as the digestive tract.

Download data

  • Downloaded 148 times
  • Download rankings, all-time:
    • Site-wide: 62,575 out of 73,470
    • In pathology: 317 out of 387
  • Year to date:
    • Site-wide: 9,250 out of 73,470
  • Since beginning of last month:
    • Site-wide: 9,250 out of 73,470

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)