Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission.
Mosquito viruses cause unpredictable outbreaks of disease. Recently, several unassigned viruses isolated from mosquitoes, including the Omono River virus (OmRV), were identified as totivirus-like viruses, with features similar to those of the Totiviridae family. Most reported members of this family...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2021-03-01
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| Series: | PLoS Pathogens |
| Online Access: | https://doi.org/10.1371/journal.ppat.1009396 |
| _version_ | 1818901883463401472 |
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| author | Qianqian Shao Xudong Jia Yuanzhu Gao Zhe Liu Huan Zhang Qiqi Tan Xin Zhang Huiqiong Zhou Yinyin Li De Wu Qinfen Zhang |
| author_facet | Qianqian Shao Xudong Jia Yuanzhu Gao Zhe Liu Huan Zhang Qiqi Tan Xin Zhang Huiqiong Zhou Yinyin Li De Wu Qinfen Zhang |
| author_sort | Qianqian Shao |
| collection | DOAJ |
| description | Mosquito viruses cause unpredictable outbreaks of disease. Recently, several unassigned viruses isolated from mosquitoes, including the Omono River virus (OmRV), were identified as totivirus-like viruses, with features similar to those of the Totiviridae family. Most reported members of this family infect fungi or protozoans and lack an extracellular life cycle stage. Here, we identified a new strain of OmRV and determined high-resolution structures for this virus using single-particle cryo-electron microscopy. The structures feature an unexpected protrusion at the five-fold vertex of the capsid. Disassociation of the protrusion could result in several conformational changes in the major capsid. All these structures, together with some biological results, suggest the protrusions' associations with the extracellular transmission of OmRV. |
| first_indexed | 2024-12-19T20:26:50Z |
| format | Article |
| id | doaj.art-b621f0fe4ac44b9a82de367f8cb384b4 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-19T20:26:50Z |
| publishDate | 2021-03-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-b621f0fe4ac44b9a82de367f8cb384b42022-12-21T20:06:49ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742021-03-01173e100939610.1371/journal.ppat.1009396Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission.Qianqian ShaoXudong JiaYuanzhu GaoZhe LiuHuan ZhangQiqi TanXin ZhangHuiqiong ZhouYinyin LiDe WuQinfen ZhangMosquito viruses cause unpredictable outbreaks of disease. Recently, several unassigned viruses isolated from mosquitoes, including the Omono River virus (OmRV), were identified as totivirus-like viruses, with features similar to those of the Totiviridae family. Most reported members of this family infect fungi or protozoans and lack an extracellular life cycle stage. Here, we identified a new strain of OmRV and determined high-resolution structures for this virus using single-particle cryo-electron microscopy. The structures feature an unexpected protrusion at the five-fold vertex of the capsid. Disassociation of the protrusion could result in several conformational changes in the major capsid. All these structures, together with some biological results, suggest the protrusions' associations with the extracellular transmission of OmRV.https://doi.org/10.1371/journal.ppat.1009396 |
| spellingShingle | Qianqian Shao Xudong Jia Yuanzhu Gao Zhe Liu Huan Zhang Qiqi Tan Xin Zhang Huiqiong Zhou Yinyin Li De Wu Qinfen Zhang Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. PLoS Pathogens |
| title | Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. |
| title_full | Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. |
| title_fullStr | Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. |
| title_full_unstemmed | Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. |
| title_short | Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. |
| title_sort | cryo em reveals a previously unrecognized structural protein of a dsrna virus implicated in its extracellular transmission |
| url | https://doi.org/10.1371/journal.ppat.1009396 |
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