Abstract: The coat protein（CP）gene of Chilli veinal mottle virus Wenchang isolate（ChiVMV-WC）was amplified by RT-PCR，and cloned into the expression vectors pET-30b（+）. After the reading frame is confirmed by sequencing, the recombinant plasmid pET30b-ChiVMV CP was transferred into E. coli Rosetta（DE3）and the expression of the recombinant CP protein was then induced by IPTG. SDS-PAGE analysis showed a high level expression of the recombinant CP of about 38 kD. The fusion protein was then purified with Ni2+-NTA agarose affinity chromatography, and used to immune rabbits for antiserum preparation. Western blot analysis confirmed that the antiserum reacted strongly and specifically to the CP of ChiVMV-WC. The optimal titer of the antiserum in indirect enzyme-linked immunosorbent assay （ID-ELISA）was determined to be 1/106. ID-ELISA testing of a number of field samples demonstrated the sensitivity and specificity of the antiserum described in this paper.

Key words: pepper, Chilli veina mottle virus, CP, prokaryotic expression, antiserum