Immunological and Morphological Properties of HBeAg Subtypes (HBeAg/1 and HBeAg/2) in Hepatitis B Virus Core Particles
| Autor: | Nakao Ishida, Shiroh Onodera, Hitoshi Ohori, Norio Shimizu, Ei Yamada |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Hepatitis B virus
Immunodiffusion Antigenicity viruses Polyacrylamide Radioimmunoassay Peptide Biology Hepatitis B Antigens Epitopes chemistry.chemical_compound Virology Humans Hepatitis B e Antigens Incubation Differential centrifugation chemistry.chemical_classification Hemagglutination virus diseases Hepatitis B digestive system diseases Molecular Weight Microscopy Electron Liver chemistry HBeAg Electrophoresis Polyacrylamide Gel Nitrocellulose |
| Zdroj: | Journal of General Virology. 65:405-414 |
| ISSN: | 1465-2099 0022-1317 |
| Popis: | A polypeptide of 21 500 mol. wt., structurally associated with hepatitis B virus core particles, was shown to have two kinds of HBeAg antigenicity (HBeAg/1 and HBeAg/2). This was revealed by transferring a single core peptide from polyacrylamide gels to nitrocellulose sheets (Western blotting), which reacted with anti-HBeAg/1 and anti-HBeAg/2. Selective discrimination of the two HBe antigens was achieved by radioimmunoassay (RIA). When highly purified core particles were incubated at 37 degrees C in a 0.1% SDS-0.1% 2-mercaptoethanol solution, only HBeAg/1 was released after 5 min incubation and the release of HBeAg/2 occurred only after prolonging incubation for 30 min. The course of degradation was also detected by CsCl density gradient centrifugation. These results indicate that HBeAg/1 is less closely associated with core particles than is HBeAg/2. Electron microscopy showed that the core particles from which HBeAg/1 was removed were more labile than the original preparation when incubated at 56 degrees C in aqueous solution, or at 37 degrees C in Sarkosyl solutions; when placed in 1 M-NaCl or -CsCl solution, the particles swelled to a larger diameter than untreated cores. |
| Databáze: | OpenAIRE |
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