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TitleDynamic rotation of the protruding domain enhances the infectivity of norovirus.
Journal, issue, pagesPLoS Pathog, Vol. 16, Issue 7, Page e1008619, Year 2020
Publish dateJul 2, 2020
AuthorsChihong 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 /
PubMed AbstractNorovirus is the major cause of epidemic nonbacterial gastroenteritis worldwide. Lack of structural information on infection and replication mechanisms hampers the development of effective vaccines ...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.
External linksPLoS Pathog / PubMed:32614892 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 13.0 Å
Structure data

EMDB-9735:
Cryo-EM structure of Murine Norovirus S7 virion with the resting P-domain conformation
Method: EM (single particle) / Resolution: 5.2 Å

EMDB-9736:
Cryo-EM structure of Murine Norovirus S7 virion with the rising P-domain conformation
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-9737:
Cryo-EM structure of Murine Norovirus 1 virion with the resting P-domain conformation
Method: EM (single particle) / Resolution: 5.3 Å

EMDB-9738:
Cryo-EM structure of Murine Norovirus 1 virion with the rising P-domain conformation
Method: EM (single particle) / Resolution: 7.3 Å

EMDB-9739:
Cryo-EM structure of Human Norovirus GII.3 VLP with the resting P-domain conformation
Method: EM (single particle) / Resolution: 9.3 Å

EMDB-9740:
Cryo-EM structure of Human Norovirus GII.3 VLP with the rising P-domain conformation
Method: EM (single particle) / Resolution: 13.0 Å

9741

6iuk

EMDB-9741: Cryo-EM structure of Murine Norovirus S7 VLP
PDB-6iuk: Cryo-EM structure of Murine Norovirus capsid
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • murine norovirus gv/nih-2410/2005/usa
KeywordsVIRUS / VLP / mature / stable

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