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<p>White spot syndrome virus (WSSV) is one of the most virulent pathogens in shrimp aquaculture. An in-depth understanding of the surface protein-protein interplays between WSSV and host is the key to further elucidating the pathogenesis mechanism. In this study, VP39A was identified as a novel cellular binding protein of WSSV by reversely conducting the biotinylation based affinity chromatography (BBAC) method. The result of indirect immunofluorescence assay, competitive ELISA, and in-vivo neutralization assays show that VP39A is vital to the cellular entry and infection of WSSV. Na<sup>+</sup>, K<sup>+</sup>-ATPase alpha subunit (NKAα), a trans-membrane subunit of complex Na<sup>+</sup>, K<sup>+</sup>-ATPase, was captured as the VP39A binding protein with pull-down assay. Co-localization of NKAα with VP39A in shrimp hemocytes was confirmed by immunofluorescence and co-immunoprecipitation studies. In addition, blocking with anti-NKAα antibody can reduce the binding of WSSV to the gill cellular membrane proteins. These results collectively demonstrate that VP39A plays an important role in the viral adsorption via its interaction with NKAα, which could be an effective target for drug design.</p>

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VP39A is a novel host cellular binding protein of white spot syndrome virus and interacts with Na+, K+-ATPase alpha subunit

  • 期刊论文

  • 发表日期：

    2025年9月6日

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  • Zengzhi Yuan,
  • Wei Ouyang,
  • Xinyi Jiang,
  • Dan Zou,
  • Xuhui Kong,
  • Jinsheng Sun

摘要

White spot syndrome virus (WSSV) is one of the most virulent pathogens in shrimp aquaculture. An in-depth understanding of the surface protein-protein interplays between WSSV and host is the key to further elucidating the pathogenesis mechanism. In this study, VP39A was identified as a novel cellular binding protein of WSSV by reversely conducting the biotinylation based affinity chromatography (BBAC) method. The result of indirect immunofluorescence assay, competitive ELISA, and in-vivo neutralization assays show that VP39A is vital to the cellular entry and infection of WSSV. Na+, K+-ATPase alpha subunit (NKAα), a trans-membrane subunit of complex Na+, K+-ATPase, was captured as the VP39A binding protein with pull-down assay. Co-localization of NKAα with VP39A in shrimp hemocytes was confirmed by immunofluorescence and co-immunoprecipitation studies. In addition, blocking with anti-NKAα antibody can reduce the binding of WSSV to the gill cellular membrane proteins. These results collectively demonstrate that VP39A plays an important role in the viral adsorption via its interaction with NKAα, which could be an effective target for drug design.