Abstract: The study was aimed to highly express NS5 protein of goose Tembusu virus （GTMUV） JS804 in Escherichia coli， then the expressed proteins was purified and characterized. The non\|structural protein 5 （NS5） gene of goose Tembusu virus in JS804 strain was amplified and cloned into expression vector pET32a（+）. The expression vector pET32a\|NS5 was then transformed into BL21 （DE3） for expression with induction of IPTG. The expressed pET32a\|NS5 products were analyzed in SDS\|PAGE and Western blotting. The molecular weight of recombinant protein NS5 was 120 ku. After 5 h induction by IPTG， the yield of fusion proteins reached peaks. The analysis showed that the fusion proteins were expressed in E.coli into inclusion bodies， and was recognized specially by rabbit anti\|Tembusu virus polyclonal antibody， which indicated a relatively high sensitivity and specificity.

Key words: goose Tembusu virus, NS5 protein, prokaryotic expression