By M. Feitelson
Since the invention of Australia antigen and its organization with variety B hepatitis, molecular characterization of the parts making up hepatitis B virus (RBV) were pursued with all over the world curiosity. during the last 20 years, such characterization has ended in the improvement of delicate assays to display and exclude infected devices from blood banks and has lately ended in the licensing of a number of RBV vaccines. That greater than 2 hundred million humans around the globe are chronically contaminated with RBV, and they are at a excessive hazard for the advance of continual hepatitis and hepatocellular carcinoma, nonetheless characterize bold difficulties in our figuring out of host-virus relationships at the molecular point. within the absence of an acceptable tissue tradition procedure, and with a really constrained host variety of an infection, characterization of RBV at the molecular point has made outstanding growth lately with the arrival of genome cloning, sequencing and expression of person virus genes through recombinant DNA expertise. The presence of hepatitis B-like viruses in an increasing variety of animal hosts, and the potential of virus replication in cells except hepatocytes, offer nice promise that destiny paintings will elucidate the molecular mechanisms operative within the a variety of results of RBV infection.
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Extra info for Molecular Components of Hepatitis B Virus
Under these conditions, one or more antigenic determinants spanning disulfide bond(s) would lose their integrity only after further modification by alkylation or exposure to denaturants such as urea. Recent experimental evidence discerning the environment around the major surface antigen polypeptides supports many of the theoretical considerations of HBsAg particle structure based upon nucleic acid and deduced amino acid sequences. Using the photoactivatable, hydrophobic probe, pyrenesulfonyl azide (PySA) in its unlabeled or tritiated form, both the major HBsAg associated polypeptides and the lipids associated with HBsAg particles were detected following SDS-PAGE by fluorescence or radioactivity (769).
The progressive unfolding of HBsAg described here is consistent with the changing immunological specificities noted when intact HBsAg was reduced or reduced and alkylated in the presence or absence of urea, and these treated forms used to raise antibodies (243). Another approach utilized to dissect the antigenic complexity of HBsAg so that immunodominant, protective determinants could better be defined on the molecular level involves the isolation of individual surface antigen associated polypeptides and their subsequent characterization by structural, antigenic and immunogenic means.
In another investigation, isolated p22-25, p26-29 and p64-72 reacted with antibodies directed against the individual polypeptides as well as HBsAg (297). General characteristics of antibodies raised against individual polypeptides include (a) induction of lower titers of anti-HBs with each polypeptide than with intact surface antigen, (b) reaction of anti-polypeptide antibodies with the homologous polypeptide more than heterologous polypeptides, (c) the presence of both group and subtype reactivity in antibodies raised against most of the HBsAg polypeptides, and (d) the indication from titration curves using anti-polypeptide antisera that p64-72 contains one or more other components in addition to the one reacting with anti-HBs.