Full—length core sequence dependent complex—type glycosylation of hepatitis C virus E2 glycoprotein

• Published in: World journal of gastroenterology : WJG Vol. 8; no. 3; pp. 499 - 504
• Main Author: Zhu, Li-Xin
• Format: Journal Article
• Language: English
• Published: United States Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China%GSF-Institut fur Molekulare Virologie,Trogerstr. 4b, 81675 Munchen, Germany. The first two authors contributed equally to this paper 01.06.2002; Baishideng Publishing Group Inc
• Subjects: Animals; Cell Line; E2糖蛋白; Glycosylation; HeLa Cells; Hepacivirus - genetics; Hepacivirus - immunology; Hepacivirus - metabolism; Hepatitis C Antibodies; Humans; Molecular Weight; Protein Processing, Post-Translational; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - genetics; Viral Envelope Proteins - metabolism; Viral Liver Diseases; 丙型肝炎病毒; 糖基化
• ISSN: 1007-9327; 2219-2840
• DOI: 10.3748/wjg.v8.i3.499

AIM：To study HCV polyprotein processing is important for the understanding of the natural history of HCV and the design of vaccines against HCV.The purpose of this study is to investigate the affection of context sequences on hepatitis C virus(HCV) E2 processing.METHODS:HCV genes of different lengths were expressed and compared in vaccinia virus/T7 system with homologous patient serum S94 and mouse anti-serum ME2116 raised against E.coli-derived E2 peptide,respectively Deglycosylation analysis and GNA(Galanthus nivalus)lectin binding assay were performed to study the posttranslational processing of the expressed products.RESULTS:E2 glycoproteins with different molecular weights (-75kDa and -60kDa)were detected using S94 and ME2116,respectively.Deglycosylation analysis showed that this difference was mainly due to different glycosylation.Endo H resistance and its failure to bind to GNA lectin demonstrated that the higher molecular weight form(75kDa)of E2 was complex-type glycosylated,which was readily recognized by homologous patient serum S94.Expression of complex-type glycosylated E2 could not be detected in all of the coretruncated constructs tested,but readily detected in constructs encoding full-length core sequences.CONCLUSION:The upstream conserved full-length core coding sequence was required for the production of E2 glycoproteins carrying complex-type N-glycans which reacted strongly with homologous patient serum and therefore possibly reprsented more mature forms of E2.As complex-type N-glycans indicated modification by Golgi enzymes,the results suggest that the presence of full-length core might be critical for E1/E2 complex to leave ER.Our data may contribute to a better understanding of the processing of HCV structural proteins as well as HCV morphogenesis.