6IUK
Cryo-EM structure of Murine Norovirus capsid
Summary for 6IUK
Entry DOI | 10.2210/pdb6iuk/pdb |
EMDB information | 9735 9736 9737 9738 9739 9740 9741 |
Descriptor | Major capsid protein VP1 (1 entity in total) |
Functional Keywords | vlp, mature, stable, virus |
Biological source | Murine norovirus GV/NIH-2410/2005/USA |
Total number of polymer chains | 3 |
Total formula weight | 176501.36 |
Authors | Song, C.,Miyazaki, N.,Iwasaki, K.,Katayama, K.,Murata, K. (deposition date: 2018-11-28, release date: 2020-02-26, Last modification date: 2024-03-27) |
Primary citation | Song, C.,Takai-Todaka, R.,Miki, M.,Haga, K.,Fujimoto, A.,Ishiyama, R.,Oikawa, K.,Yokoyama, M.,Miyazaki, N.,Iwasaki, K.,Murakami, K.,Katayama, K.,Murata, K. Dynamic rotation of the protruding domain enhances the infectivity of norovirus. Plos Pathog., 16:e1008619-e1008619, 2020 Cited by PubMed Abstract: 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 resting conformation in this process. Furthermore, in the resting conformation, the cellular receptor CD300lf is readily accessible, and thus infection efficiency is significantly enhanced. Two similar P domain conformations were also found simultaneously in the human norovirus GII.3 capsid, although the mechanism of the conformational change is not yet clear. These results provide new insights into the mechanisms of non-enveloped norovirus transmission that invades host cells, replicates, and sometimes escapes the hosts immune system, through dramatic environmental changes in the gastrointestinal tract. PubMed: 32614892DOI: 10.1371/journal.ppat.1008619 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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