Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules
A previous study found the key transcription factor of Litopenaeus vannamei PERK-eIF2α pathway cyclic AMP-dependent transcription factor 4 (LvATF4) was involved in the transcriptional regulation of white spot syndrome virus (WSSV) gene wsv023. Knocked-down expression of LvATF4 reduced the viral copy...
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The Royal Society
2017-01-01
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| Series: | Royal Society Open Science |
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| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.160379 |
| _version_ | 1818458662521274368 |
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| author | Yihong Chen Haitao Bi Xiaoyun Li Zezhi Zhang Haitao Yue Shaoping Weng Jianguo He |
| author_facet | Yihong Chen Haitao Bi Xiaoyun Li Zezhi Zhang Haitao Yue Shaoping Weng Jianguo He |
| author_sort | Yihong Chen |
| collection | DOAJ |
| description | A previous study found the key transcription factor of Litopenaeus vannamei PERK-eIF2α pathway cyclic AMP-dependent transcription factor 4 (LvATF4) was involved in the transcriptional regulation of white spot syndrome virus (WSSV) gene wsv023. Knocked-down expression of LvATF4 reduced the viral copy number and the cumulative mortality of WSSV-infected shrimp. These results suggested that wsv023 may be critical to WSSV infection but the precise function of wsv023 was still unknown. By using co-immunoprecipitation and pull-down assays, we show that wsv023 interacts with L. vannamei gamma complex-associated protein 2 (LvGCP2), which is the core protein of the γ-tubulin small complex. Knocked-down, the wsv023 gene significantly reduced the copy number of WSSV in L. vannamei muscle, as well as the cumulative mortality of infected shrimp. And PERK-eIF2α pathway inhibition also showed reduced virus copy number and abrogated shrimp mortality. Furthermore, overexpression of wsv023 inhibited the formation of microtubules in 293T cells. Flow cytometry revealed that WSSV infection similarly decreased the formation of microtubules in L. vannamei haemocytes. These findings suggested that wsv023 plays a role in microtubule organization in host cells, which in turn may be beneficial to WSSV. |
| first_indexed | 2024-12-14T23:02:01Z |
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| id | doaj.art-31b93bc410c44623b22a4155d43f1770 |
| institution | Directory Open Access Journal |
| issn | 2054-5703 |
| language | English |
| last_indexed | 2024-12-14T23:02:01Z |
| publishDate | 2017-01-01 |
| publisher | The Royal Society |
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| series | Royal Society Open Science |
| spelling | doaj.art-31b93bc410c44623b22a4155d43f17702022-12-21T22:44:25ZengThe Royal SocietyRoyal Society Open Science2054-57032017-01-014410.1098/rsos.160379160379Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubulesYihong ChenHaitao BiXiaoyun LiZezhi ZhangHaitao YueShaoping WengJianguo HeA previous study found the key transcription factor of Litopenaeus vannamei PERK-eIF2α pathway cyclic AMP-dependent transcription factor 4 (LvATF4) was involved in the transcriptional regulation of white spot syndrome virus (WSSV) gene wsv023. Knocked-down expression of LvATF4 reduced the viral copy number and the cumulative mortality of WSSV-infected shrimp. These results suggested that wsv023 may be critical to WSSV infection but the precise function of wsv023 was still unknown. By using co-immunoprecipitation and pull-down assays, we show that wsv023 interacts with L. vannamei gamma complex-associated protein 2 (LvGCP2), which is the core protein of the γ-tubulin small complex. Knocked-down, the wsv023 gene significantly reduced the copy number of WSSV in L. vannamei muscle, as well as the cumulative mortality of infected shrimp. And PERK-eIF2α pathway inhibition also showed reduced virus copy number and abrogated shrimp mortality. Furthermore, overexpression of wsv023 inhibited the formation of microtubules in 293T cells. Flow cytometry revealed that WSSV infection similarly decreased the formation of microtubules in L. vannamei haemocytes. These findings suggested that wsv023 plays a role in microtubule organization in host cells, which in turn may be beneficial to WSSV.https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.160379unfolded protein responselitopenaeus vannameiwhite spot syndrome viruswsv023 |
| spellingShingle | Yihong Chen Haitao Bi Xiaoyun Li Zezhi Zhang Haitao Yue Shaoping Weng Jianguo He Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules Royal Society Open Science unfolded protein response litopenaeus vannamei white spot syndrome virus wsv023 |
| title | Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules |
| title_full | Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules |
| title_fullStr | Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules |
| title_full_unstemmed | Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules |
| title_short | Wsv023 interacted with Litopenaeus vannamei γ-tubulin complex associated proteins 2, and decreased the formation of microtubules |
| title_sort | wsv023 interacted with litopenaeus vannamei γ tubulin complex associated proteins 2 and decreased the formation of microtubules |
| topic | unfolded protein response litopenaeus vannamei white spot syndrome virus wsv023 |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.160379 |
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