## Abstract The genotype of hepatitis C virus (HCV) can profoundly affect the success of antiviral therapy for HCV infection. A possible contributing factor is a varied immune response elicited by infection with different HCV genotypes. In this study, fullβlength E2 proteins of HCV genotypes 1a, 1b
A model for the hepatitis C virus envelope glycoprotein E2
β Scribed by Asutosh T. Yagnik; Armin Lahm; Annalisa Meola; Rosa Maria Roccasecca; Bruno B. Ercole; Alfredo Nicosia; Anna Tramontano
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 671 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The significance of circulating antibody to hepatitis C HCV E1 corresponds to the pestiviral gp33/gp25 envevirus (HCV) envelope glycoprotein 2 (E2)/nonstructural lope glycoprotein and the flaviviral envelope protein protein 1 (NS1) glycoprotein was studied in 83 patients (M/E), whereas E2/NS1 corres
Our previous studies demonstrated that hepatitis C virus (HCV) envelope glycoproteins 1 and 2 (E1 and E2) display distinct reactivity to different cell-surface molecules. In this study, we characterized the interaction of E1 and E2 with apolipoproteins in facilitating virus entry. The results sugges
The second envelope protein (E2) of the hepatitis C virus (HCV) was cloned and expressed in Chinese hamster ovary (CHO) cells. This E2 glycoprotein was purified using ion exchange and lectin chromatography and used to construct an enzyme immunoassay for HCV E2 antibodies. The assay was shown to have
The hepatitis C virus (HCV) envelope glycoprotein E1 has been widely employed as a potential vaccine antigen in clinical research. A truncated form (amino acids 192-326) of the E1 protein (E1y) was expressed in the yeast Hansenula polymorpha and purified from the cell lysate. E1y forms protein parti
Subviral particles of hepatitis B virus have been used to present foreign epitopes. We attempted to present the hydrophilic domains of E2 envelope protein of hepatitis C virus (HCV) as a fusion protein with hepatitis B virus surface antigen (HBsAg). The five hydrophilic domains of HCV E2 antigen wer