CONSTRUCTION AND EXPRESSION OF PROKARYOTIC EXPRESSIVE CLONE OF HUMAN HERPES VIRUS 6 101K TEGUMENT PROTEIN MAJOR ANTIGEN EPITOPES

ObjectiveTo construct prokaryotic expression clones of human herpes virus 6(HHV-6) 101K protein genes.MethodsA fragment coding for HHV-6 101K major antigen epitopes(666-843 aa) was amplified by PCR technique.The PCR products were cloned into TA cloning vector for sequencing and subsequently compared with the sequence of HHV-6B Z29 strain in GeneBank.The target gene was inserted into the prokaryotic expression plasmid pThioHis A.After the transformation of E.coli BL21,the recombinant plasmid was induced with IPTG to express the 101K fusion proteins.Recombinant prokaryotic expression plasmid was confirmed by PCR and restricted endonuclease analysis and the recombinant protein was confirmed by SDS-PAGE.(ResultsThe) sequence of the target gene was identical with that of HHV-6B Z29 strain in GenBank.The relative molecular weight 31 900 fusion proteins were expressed in E.coli BL21.ConclusionThe successful construction of recombinant prokaryotic expression plasmid and expression of the recombinant protein provides valuable information for the diagnosis of active HHV-6 infection.