Objective:To clone and express the ORF50 truncated genes and the full length vIL-6 gene of human herpesvirus 8(HHV-8 ) in E.coli, and purify vIL-6/GST fusion protein. Methods:Three pairs of PCR primers were designed according to 3’ends of ORF50 gene encoding C-terminal amino acids(aa 525-691, aa 513-660, aa 541-691), and a pair of PCR primers was also designed according to the full length vIL-6 gene. The DNA of plasmid pcDNA3.1+ORF50 or pcDNA3.1+vIL-6 was taken as a template, and the genes were amplified using PCR. Subsequently, amplified gene fragments were digested with the restriction enzymes and then cloned into pGEX-6p-1 with proper reading frame to create recombinant prokaryotic expression plasmids designated as pORF50-C1,pORF50-C2,pORF50-C3 and pvIL-6. After identification with enzyme digestion and nucleotide sequences analysis, the recombinant prokaryotic expression plasmids were transformed into host BL21(DE3) cells. The GST fusion protein expression was induced with isopropyl-β-D-thiogalactopyranoside(IPTG). The vIL-6 fusion protein was purified by chromatography Glutathione Sepharose 4B. The expression and the purification of the fusion proteins were detected by SDS-PAGE and Western blot. Results:The isolated sequences were 100% homology with the aimed genes registered in GenBank. The fusion proteins could be detected by SDS-PAGE and Western blot as expected. Conclusion:The ORF50 truncated genes and the full length vIL-6 gene were correctly expressed in E.coli BL21 (DE3)cells. The vIL-6/GST fusion protein was successfully purified.