Immunological and morphological properties of HBeAg subtypes (HBeAg/1 and HBeAg/2) in hepatitis B virus core particles.
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.
D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000032:analysis; D006384:Hemagglutination; D006509:Hepatitis B / Q000382:microbiology; D006511:Hepatitis B Antigens / Q000302:isolation & purification*; D006513:Hepatitis B e Antigens / Q000302:isolation & purification*; D006515:Hepatitis B virus / Q000276:immunology*; D006801:Humans; D005779:Immunodiffusion; D008099:Liver / Q000382:microbiology; D008854:Microscopy, Electron; D008970:Molecular Weight; D011863:Radioimmunoassay
D000939:Epitopes; D006511:Hepatitis B Antigens; D006513:Hepatitis B e Antigens