Abstract: In this study,HN gene of Newcastle disease virus(NDV) isolate sc05 was cloned,sequenced,on this basis,the 76 to 571 aa fragment of C-terminal function domain was subcloned into pET32a(＋) expression vector,obtained recombinant expression plasmid pET32a-HN. pET32a-HN was identificated to be correct, and it was transfored into BL21 plysS(DE3) cells. Selected positive clones, induced expression by 1 mmol/L IPTG, and the expression products were identified. SDS-PAGE electrophoresis showed that HN gene function domain fragments in BL21 plysS(DE3) cells achieved fusion expression, size of the recombinant protein was about 76 ku, Western blotting confirmed the biological activity of recombinant protein. This work was benefit for further study of the functional domains of the HN protein immunogenicity and the development of the HN gene of Newcastle disease vaccine project.

Key words: NDV; HN gene; clone; function domain; prokaryotic expression