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KMID : 0578319950050060563
Molecules and Cells
1995 Volume.5 No. 6 p.563 ~ p.568
Characterization of the Putative E2 Envelope Glycoprotein of hepatitis C Virus Expressed in Stably Transformed Chinese Hamster Ovary Cells
Ryu, Wang-Shick
Choi, Deong-Dyoung/Yang, Jae-Young/Kim, Chun-Hyung/Kwon, Wyoung-Sun/So, Hong-Seob/Cho, Joong Myung
Abstract
We established a Chinese hamster ovary (CHO) cell line that stably expressed E2 envelope glycoprotein of hepatitis C virus. E2 glycoprotein was stably expressed in the cell, but not secreted into culture medium. To examine the extent of cellular processing, biochemical properties of the E2 glycoprotein were examined by deglycosylation analysis, lectin affinity chromatography, and sedimentation analysis. Our results showed that (¥¡) the E2 glycoprotein was heavily glycosylated, (¥¢) it was endo-H sensitive, (¥£) it bound to a Galanthus nivalus agarose lectin column, and (¥¤) it existed as a monomer in the cell as evidenced by sedimentation analysis. These biochemical properties indicated that the processing of E2 glycoprotein was blocked at the endoplasmin reticulum. It will be of interest to determine whether E2 glycoprotein derived from the CHO cell line could elicit neutralizing antibody in an animal model.
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