HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Kohara, M. Articles by Nomoto, A. Search for Related Content PubMed PubMed Citation Articles by Kohara, M. Articles by Nomoto, A. Agricola Articles by Kohara, M. Articles by Nomoto, A.

Expression and characterization of glycoprotein gp35 of hepatitis C virus using recombinant vaccinia virus

¹ Fundamental Research Laboratory, Corporate Research and Development Laboratory, Tonen Co. Nishi-Tsurugaoka, Ohi-machi, Iruma-gun, Saitama 354
² Department of Microbiology, The Tokyo Metropolitan Institute of Medical Science
and The³ Tokyo Metropolitan Komagome Hospital, Honkomagome, Bunkyo-ku, Tokyo 113
⁴ Department of Veterinary Science
and⁵ Department of Enteroviruses, National Institute of Health, Kamiosaki, Shinagawa-ku, Tokyo 141, Japan

Complementary DNA clones corresponding to one of the putative structural regions of the hepatitis C virus (HCV) genome were obtained from sera of non-A non-B hepatitis patients. The putative envelope gene was expressed by using a recombinant vaccinia virus carrying this region of the HCV genome. In cells infected with the recombinant vaccinia virus, a glycosylated protein with an M_r of about 35K (gp35) was specifically detected by convalescent sera from hepatitis C patients. The sera from rabbits immunized with this recombinant vaccinia virus reacted to the gp35 produced in insect cells and also to gp35 which was translated in vitro in the glycosylated and processed form. The gp35 was used to detect antibodies in sera of only 7 to 23% of HCV patients at various stages of HCV disease. These results suggest that the gp35 of HCV may not have high antigenicity in humans.

Received 9 March 1992; accepted 1 June 1992.

This article has been cited by other articles:

				J. Meunier, A Fournillier, A Choukhi, A Cahour, L Cocquerel, J Dubuisson, and C Wychowski Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex J. Gen. Virol., April 1, 1999; 80(4): 887 - 896. [Abstract]

				K. Yasui, T. Wakita, K. Tsukiyama-Kohara, S.-I. Funahashi, M. Ichikawa, T. Kajita, D. Moradpour, J. R. Wands, and M. Kohara The Native Form and Maturation Process of Hepatitis C Virus Core Protein J. Virol., July 1, 1998; 72(7): 6048 - 6055. [Abstract] [Full Text] [PDF]