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Dynamic rotation of the protruding domain enhances the infectivity of norovirus
- Source :
- PLoS Pathogens, PLoS Pathogens, Vol 16, Iss 7, p e1008619 (2020)
- Publication Year :
- 2020
- Publisher :
- Public Library of Science, 2020.
-
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.<br />Author summary The capsid structure of caliciviruses has been reported to be classified into two different types, according to the species and genotype. One is the rising type of P domain conformation as shown in human norovirus GII.10 and rabbit hemorrhagic disease virus (RHDV), where the P domain rises from the S domain surface. The other is the resting type of P domain conformation as shown in human norovirus GI.1, sapovirus and San Miguel sea lion virus (SMSV), where the P domain rests upon the S domain. Here, we demonstrate that the P domain of the murine noroviruses changes reversibly between the rising and resting P domain conformation types in response to aqueous conditions. We also found the similar two P domain conformations in human norovirus GII.3 VLPs at the same time. Our findings provide new insights into the mechanisms of viral infection of caliciviruses.
- Subjects :
- RNA viruses
Conformational change
Viral Diseases
viruses
ved/biology.organism_classification_rank.species
Pathology and Laboratory Medicine
medicine.disease_cause
Viral Packaging
Mice
fluids and secretions
Medicine and Health Sciences
Electron Microscopy
Biology (General)
Materials
Infectivity
0303 health sciences
Microscopy
biology
Chemistry
030302 biochemistry & molecular biology
Monomers
virus diseases
Infectious Diseases
Capsid
Medical Microbiology
Viral Pathogens
Physical Sciences
Viruses
Pathogens
Research Article
QH301-705.5
Immunology
Protein domain
Materials Science
Viral Structure
Research and Analysis Methods
Microbiology
Caliciviruses
Virus
Cell Line
Domain (software engineering)
03 medical and health sciences
Immune system
Protein Domains
Virology
Genetics
medicine
Animals
Humans
Dimers
Molecular Biology
Microbial Pathogens
030304 developmental biology
ved/biology
Norovirus
Host Cells
Organisms
Biology and Life Sciences
Calicivirus Infection
Electron Cryo-Microscopy
Sapovirus
RC581-607
Polymer Chemistry
biology.organism_classification
Viral Replication
Cell culture
Oligomers
Biophysics
Parasitology
Capsid Proteins
Immunologic diseases. Allergy
Viral Transmission and Infection
Function (biology)
Murine norovirus
Subjects
Details
- Language :
- English
- ISSN :
- 15537366
- Volume :
- 16
- Issue :
- 7
- Database :
- OpenAIRE
- Journal :
- PLOS Pathogens
- Accession number :
- edsair.doi.dedup.....e474e14b605ecefe92bd92906ec1d350