Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
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
_version_ 1783553434306215936
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
work_keys_str_mv AT songchihong dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT takaitodakareiko dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT mikimotohiro dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT hagakei dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT fujimotoakira dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT ishiyamaryoka dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT oikawakazuki dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT yokoyamamasaru dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT miyazakinaoyuki dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT iwasakikenji dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT murakamikosuke dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT katayamakazuhiko dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus
AT muratakazuyoshi dynamicrotationoftheprotrudingdomainenhancestheinfectivityofnorovirus