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Dynamic rotation of the protruding domain enhances the infectivity of norovirus
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 norovi...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7331980/ https://www.ncbi.nlm.nih.gov/pubmed/32614892 http://dx.doi.org/10.1371/journal.ppat.1008619 |
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author | Song, Chihong Takai-Todaka, Reiko Miki, Motohiro Haga, Kei Fujimoto, Akira Ishiyama, Ryoka Oikawa, Kazuki Yokoyama, Masaru Miyazaki, Naoyuki Iwasaki, Kenji Murakami, Kosuke Katayama, Kazuhiko Murata, Kazuyoshi |
author_facet | Song, Chihong Takai-Todaka, Reiko Miki, Motohiro Haga, Kei Fujimoto, Akira Ishiyama, Ryoka Oikawa, Kazuki Yokoyama, Masaru Miyazaki, Naoyuki Iwasaki, Kenji Murakami, Kosuke Katayama, Kazuhiko Murata, Kazuyoshi |
author_sort | Song, Chihong |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7331980 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-73319802020-07-14 Dynamic rotation of the protruding domain enhances the infectivity of norovirus Song, Chihong Takai-Todaka, Reiko Miki, Motohiro Haga, Kei Fujimoto, Akira Ishiyama, Ryoka Oikawa, Kazuki Yokoyama, Masaru Miyazaki, Naoyuki Iwasaki, Kenji Murakami, Kosuke Katayama, Kazuhiko Murata, Kazuyoshi PLoS Pathog Research Article 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. Public Library of Science 2020-07-02 /pmc/articles/PMC7331980/ /pubmed/32614892 http://dx.doi.org/10.1371/journal.ppat.1008619 Text en © 2020 Song et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Song, Chihong Takai-Todaka, Reiko Miki, Motohiro Haga, Kei Fujimoto, Akira Ishiyama, Ryoka Oikawa, Kazuki Yokoyama, Masaru Miyazaki, Naoyuki Iwasaki, Kenji Murakami, Kosuke Katayama, Kazuhiko Murata, Kazuyoshi Dynamic rotation of the protruding domain enhances the infectivity of norovirus |
title | Dynamic rotation of the protruding domain enhances the infectivity of norovirus |
title_full | Dynamic rotation of the protruding domain enhances the infectivity of norovirus |
title_fullStr | Dynamic rotation of the protruding domain enhances the infectivity of norovirus |
title_full_unstemmed | Dynamic rotation of the protruding domain enhances the infectivity of norovirus |
title_short | Dynamic rotation of the protruding domain enhances the infectivity of norovirus |
title_sort | dynamic rotation of the protruding domain enhances the infectivity of norovirus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7331980/ https://www.ncbi.nlm.nih.gov/pubmed/32614892 http://dx.doi.org/10.1371/journal.ppat.1008619 |
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