Journal of Veterinary Science

  • 제21권2호
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  • Pages.33.1-33.15
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  • 2020
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  • 1229-845X(pISSN)
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  • 1976-555X(eISSN)
대한수의학회 (The Korean Society of Veterinary Science)
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Annexin A2 gene interacting with viral matrix protein to promote bovine ephemeral fever virus release

  • Chen, Lihui (Ruminant Diseases Research Center, College of Life Sciences, Shandong Normal University) ;
  • Li, Xingyu (Ruminant Diseases Research Center, College of Life Sciences, Shandong Normal University) ;
  • Wang, Hongmei (Ruminant Diseases Research Center, College of Life Sciences, Shandong Normal University) ;
  • Hou, Peili (Ruminant Diseases Research Center, College of Life Sciences, Shandong Normal University) ;
  • He, Hongbin (Ruminant Diseases Research Center, College of Life Sciences, Shandong Normal University)
  • 투고 : 2019.09.03
  • 심사 : 2019.12.30
  • 발행 : 2020.03.31
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초록

Bovine ephemeral fever virus (BEFV) causes bovine ephemeral fever, which can produce considerable economic damage to the cattle industry. However, there is limited experimental evidence regarding the underlying mechanisms of BEFV. Annexin A2 (AnxA2) is a calcium and lipid-conjugated protein that binds phospholipids and the cytoskeleton in a Ca2+-dependent manner, and it participates in various cellular functions, including vesicular trafficking, organization of membrane domains, and virus proliferation. The role of the AnxA2 gene during virus infection has not yet been reported. In this study, we observed that AnxA2 gene expression was up-regulated in BHK-21 cells infected with the virus. Additionally, overexpression of the AnxA2 gene promoted the release of mature virus particles, whereas BEFV replication was remarkably inhibited after reducing AnxA2 gene expression by using the small interfering RNA (siRNA). For viral proteins, overexpression of the Matrix (M) gene promotes the release of mature virus particles. Moreover, the AnxA2 protein interaction with the M protein of BEFV was confirmed by GST pull-down and co-immunoprecipitation assays. Experimental results indicate that the C-terminal domain (268-334 aa) of AxnA2 contributes to this interaction. An additional mechanistic study showed that AnxA2 protein interacts with M protein and mediates the localization of the M protein at the plasma membrane. Furthermore, the absence of the AnxA2-V domain could attenuate the effect of AnxA2 on BEFV replication. These findings can contribute to elucidating the regulation of BEFV replication and may have implications for antiviral strategy development.

키워드

과제정보

This study was partially supported by grants from the National Natural Science Fund of China (31872490, 31672556), the Primary Research & Development Plan of Shandong Province (2018GNC113011), and a fund earmarked for the Taishan Scholar Project (Hongbin He).

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