Envelope proteins of white spot syndrome virus (WSSV) play an important role in viral entry as well as in triggering host defences. To date, some main envelope proteins such as VP28, VP24 and VP19 have been expressed heterologously and proved effective in WSSV prevention. However, VP62, an envelope protein with hub function as well as better antigenicity, has not been focused on. In an attempt to prepare this protein for rapid purification and further functional analysis, N‐terminus‐truncated VP62 was expressed in Escherichia coli using two common fusion tags, including hexahistidine (his6) and solubility‐enhancing tag thioredoxin (Trx). The results showed that the truncated VP62 fused with C‐terminal His‐tag could not be expressed in either E. coli BL21(Plyss) or Arctic Express, but it could be expressed in the form of inclusion bodies in Arctic Express with N‐terminal tag. After refolding and His‐tag affinity purification, the protein with purity over 90% was obtained. This study laid the foundation for evaluation of its vaccine potential as well as further application in WSSV prevention.

中文翻译：

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具有疫苗潜力的白斑综合症病毒中枢蛋白的原核表达

白斑综合症病毒（WSSV）的包膜蛋白在病毒进入以及触发宿主防御中起着重要作用。迄今为止，一些主要的包膜蛋白，例如VP28，VP24和VP19已经异源表达，并被证明在预防WSSV中有效。然而，VP62是一种具有集线器功能以及更好的抗原性的包膜蛋白，目前尚未得到关注。为了准备将该蛋白用于快速纯化和进一步的功能分析，使用两种常见的融合标签，包括六组氨酸（his6）和溶解度增强标签硫氧还蛋白（Trx），在大肠杆菌中表达了N末端截短的VP62 。结果表明，截短的VP62与C末端His-tag融合不能在两种大肠杆菌中表达BL21（Plyss）或Arctic Express，但可以在带有N末端标签的Arctic Express中以包含体的形式表示。重新折叠并进行His-tag亲和纯化后，获得的蛋白纯度超过90％。该研究为评估其疫苗潜力以及进一步预防WSSV奠定了基础。