By M. Feitelson
Since the invention of Australia antigen and its organization with style B hepatitis, molecular characterization of the elements making up hepatitis B virus (RBV) were pursued with world wide curiosity. during the last twenty years, such characterization has ended in the advance of delicate assays to monitor and exclude infected devices from blood banks and has lately led to the licensing of numerous RBV vaccines. That greater than two hundred million humans world wide are chronically contaminated with RBV, and they are at a excessive chance for the advance of persistent hepatitis and hepatocellular carcinoma, nonetheless signify bold difficulties in our realizing of host-virus relationships at the molecular point. within the absence of an acceptable tissue tradition procedure, and with a truly constrained host variety of an infection, characterization of RBV at the molecular point has made outstanding development lately with the appearance of genome cloning, sequencing and expression of person virus genes by means of recombinant DNA expertise. The presence of hepatitis B-like viruses in an increasing variety of animal hosts, and the potential for 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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Additional info for Molecular Components of Hepatitis B Virus
Each expression pattern predominates in different forms of chronic hepatitis; (D) HB associated antigens and antibodies in blood. [Reprinted by permission from Bianchi, F. and F. Gudat in Progress in Liver Disease, Vol. 4, Chapter 20, pp. 371-392. Copyright 1979 by Grune & Stratton, Inc. (ref. 348)J. immunogenic form, several polypeptide vaccines consisting of p22-25 and p26-29 isolated from preparative SDS gels (351, 352, 355) or by Triton X-lOa treatment of HBsAg particles (350) were used as starting material.
NG1ycoproteins detected b~ virtue of carbohydrate(s) labeled w~th tritiated sodium borohydride. OPo1ypeptides labeled by 5S-methionine and immunoprecipitated prior to SDS-PAGE. PG1ycoproteins detected by virtue of tritiated sugars incorporated into metabolically labeled HBsAg. QPo1ypeptides labeled metabolically uSin~ tritiated amino acids. rpo1ypeptide gel profile deduced from 12 I-labeled components using iodogen. Table 4. 30 acid residues of cysteine in p25 (Table 5), the failure to resolve the major surface antigen polypeptides on SDS polyacrylamide gels in the absence of a reducing agent (292), and the resistance of HBsAg particles, even in the presence of 6M urea or 1% SDS, to undergo carboxymethylation, suggest that most if not all of the cysteine residues present in p25 are involved in disulfide bonding.
These results suggest that antibodies raised against residues 2-16, 22-35 and 95-109 recognize and bind to exposed regions of beta sheet structure in the amino terminal portion of the molecule, as well as to the minor hydrophilic domain of HBsAg polypeptide (residues 48-81), but not to regions in the carboxy terminal portion of the molecule. These results may be indicative of an exposed amino terminus and buried carboxy terminus in intact particles. The finding of anti-peptide immunoglobulin following immuniza- tion with residues 38-52, 47-52 and 104-109, which did not bind to intact surface antigen, suggests that these regions are not exposed on the surface of HBsAg; but lack of appropriate peptide conformation might also have contributed to these results.