By M. Feitelson
Since the invention of Australia antigen and its organization with variety B hepatitis, molecular characterization of the elements making up hepatitis B virus (RBV) were pursued with around the world curiosity. during the last 20 years, such characterization has resulted in the improvement of delicate assays to monitor and exclude infected devices from blood banks and has lately ended in the licensing of numerous RBV vaccines. That greater than 2 hundred million humans world wide are chronically contaminated with RBV, and they are at a excessive danger for the improvement of power hepatitis and hepatocellular carcinoma, nonetheless characterize ambitious difficulties in our knowing of host-virus relationships at the molecular point. within the absence of an acceptable tissue tradition process, and with a truly constrained host variety of an infection, characterization of RBV at the molecular point has made impressive development lately with the arrival of genome cloning, sequencing and expression of person virus genes by way of recombinant DNA know-how. The presence of hepatitis B-like viruses in an increasing variety of animal hosts, and the opportunity of virus replication in cells except hepatocytes, offer nice promise that destiny paintings will elucidate the molecular mechanisms operative within the quite a few results of RBV infection.
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Extra resources for Molecular Components of Hepatitis B Virus
JPolypeptide gel profile deduced from 125 1 labeled components radioacylated with the Bolton-Hunter reagent (267). kImmunogenicity (anti-HBs) to HBsAg demonstrated from animals injected with indicated polypeptide. lImmunogenicity (cellular response) to HBsAg demonstrated from animals injected with indicated polypeptide. mMajor component released from HBsAg treated with 1% SDS and 65mM DTT. nG1ycoproteins detected b~ virtue of carbohydrate(s) labeled w~th tritiated sodium borohydride. OPo1ypeptides labeled by 5S-methionine and immunoprecipitated prior to SDS-PAGE.
The presence of a larger than average percentage of tryptophan in HBsAg and its tendency in helical structures to be associated with alpha helix formation, also suggests a high percentage of this type of secondary structure. The very high percentage of serine residues in HBsAg, which is interesting because serine tends to disrupt beta secondary structure, is also consistent with the above results, suggesting high alpha helical content in intact surface antigen particles and with the ORD and CD spectra discussed above, which also indicate high alpha helical content (242).
Further, the anti-HBs titers elicited by the polypeptides were often 37 2-3 orders of magnitude lower in titer than using equivalent amounts of RBsAg, again suggesting partial renaturation, but also indicating that the presence of repeating antigenic determinants may be important in elucidating a high titer of anti-RBs (208, 263). Although some studies describe a failure of p26-29, the major glycosylated component, to elicit anti-RBs (203, 207), other studies claim this polypeptide to be the most immunogenic (202, 208, 209, 296, 297).