The E7 gene of human papillomavirus type 16 was expressed in E. coli with molecular cloning technique. A 191 bp fragment containing most of the E7 gene was cut out from the HPV 16 genome with the restriction enzyme Dde Ⅰ. The plasmid pATH10 which contains the promoter of the tryptophane operon was chosen as the expression vector. The 191 bp fragment and the vector plasmid were ligated together later and the recombinant DNA formed was used to transform E. coli DH5α. Restriction enzyme mapping and SDS-PAGE protein analysis were done on four transformants. The molecular weight of the newly expressed protein of the transformant was estimated and found to correspond well with that expected theoretically. We concluded that the expressed protein was a fusion protein of TrpE/E7_32-95aa.