A method for obtaining a subunit inactivated vaccine preparation from the 22-nm particles of HBsAg is proposed. For inactivation of the residual infectious hepatitis B virus (HBV) the preparations were successively treated with 1% sodium dodecyl sulfate (SDS) and nucleases. In addition, thermal dena
Polyalbumin receptors on hepatitis B virus and on 22 nm hepatitis B surface antigen (H BsAg)2 particles
β Scribed by P. Pontisso; E. Falcieri; E. Schiavon; Dr. A. Alberti; G. Realdi
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- English
- Weight
- 443 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0146-6615
No coin nor oath required. For personal study only.
β¦ Synopsis
Receptors for polymerized human serum albumin ( pHSA ) were studied by solid-phase radioimmunoassay on different hepatitis B surface antigen (HBsAg) particles subpopulations prepared both from hepatitis B e antigen (HBeAg) and from anti-HBe-positive sera. HBsAg particles in HBeAg-positive serum showed higher expression of the receptor compared with HBsAg particles from anti-HBe-positive serum. Analysis of different morphological forms of virus particles was performed after separation by density-gradient ultracentrifugation. Maximum receptor expression was detected in HBV particles containing fractions while the 22-nm HBsAg particles had significantly lower receptor activity. These observations support the hypothesis of a pathogenetic role of the pHSA receptor in mediating virus access to hepatocytes. Indeed, the higher pHSA binding activity on HBV particles could allow selective attachment of the infectious virion to liver cells that bear similar albumin receptors on their surface.
π SIMILAR VOLUMES
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
## Abstract Amino acid changes within the major antigenic determinant of the hepatitis B virus (HBV) surface antigen (HBsAg) may modify eventually the antigenic properties of the protein and may have impact on the sensitivity of diagnostic assays. Modifications in the design of an assay can, howeve
mines the outcome after OLT in patients on high dose HBIg Hepatitis B virus (HBV) infection of the liver graft is a major prophylaxis. (HEPATOLOGY 1997;26:478-484.) complication after orthotopic liver transplantation (OLT) for HBV-related cirrhosis. A high viral load before OLT is a known risk facto
Receptors for polymerised human albumin are present on the pre-S sequence of the envelope protein of HBV and on the hepatocyte membrane and are thought to be involved in uptake of the virus by hepatocytes. Using a solid phase radioimmunoassay we demonstrate binding of HBsAg to polymerised human seru