Abstract
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.
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