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首页> 外文期刊>Archives of virology >Tetramerization of white spot syndrome virus envelope protein VP33 and its interaction with VP24.
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Tetramerization of white spot syndrome virus envelope protein VP33 and its interaction with VP24.

机译:白斑综合症病毒包膜蛋白VP33的四聚化及其与VP24的相互作用。

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VP33, also termed VP281, VP37 or VP36B, is a minor envelope protein of white spot syndrome virus (WSSV). Because of its low abundance and lack of a transmembrane domain, we hypothesized that VP33 is likely to be attached to the viral envelope by interaction with other envelope proteins. In this study, we employed far-western blotting and pull-down assays to demonstrate that VP33 interacts with itself, as well as with VP24, which is one of the four major viral envelope proteins. Moreover, a gel-filtration analysis was performed to show that this self-interaction led to the formation of stable VP33 tetramers. These results implied that VP33 tetramers were anchored to the viral envelope through interaction with VP24, suggesting that VP33 may participate in the formation of the WSSV envelope.
机译:VP33,也称为VP281,VP37或VP36B,是白斑综合症病毒(WSSV)的次要包膜蛋白。由于其丰度低和缺乏跨膜结构域,我们假设VP33可能通过与其他包膜蛋白相互作用而附着在病毒包膜上。在这项研究中,我们采用了远古印迹和下拉测定法来证明VP33与自身以及与VP24(四种主要的病毒包膜蛋白之一)相互作用。此外,进行了凝胶过滤分析以表明这种自相互作用导致形成稳定的VP33四聚体。这些结果表明,VP33四聚体通过与VP24相互作用而锚定在病毒包膜上,表明VP33可能参与了WSSV包膜的形成。

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