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Polyalbumin receptors on hepatitis B virus and on 22 nm hepatitis B surface antigen (H BsAg) 2 particles
Author(s) -
Pontisso P.,
Falcieri E.,
Schiavon E.,
Alberti A.,
Realdi G.
Publication year - 1984
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.1890130406
Subject(s) - hbsag , hbeag , hepatitis b virus , receptor , virology , antigen , hepadnaviridae , hepatitis b , virus , radioimmunoassay , microbiology and biotechnology , chemistry , biology , immunology , biochemistry
Receptors for polymerized human serum albumin (pHSA) were studied by solidphase radioimmunoassay on different hepatitis B surface antigen (HBsAg) particles subpopulations prepared both from hepatitis B e antigen (HBeAg) and from anti‐HBe‐positive sera. HBsAg particles in HBeAg‐positive serum showed higher expression of the receptor compared with HBsAg particles from anti‐HBe‐positive serum. Analysis of different morphological forms of virus particles was performed after separation by density‐gradient ultracentrifugation. Maximum receptor expression was detected in HBV particles containing fractions while the 22‐nm HBsAg particles had significantly lower receptor activity. These observations support the hypothesis of a pathogenetic role of the pHSA receptor in mediating virus access to hepatocytes. Indeed, the higher pHSA binding activity on HBV particles could allow selective attachment of the infectious virion to liver cells that bear similar albumin receptors on their surface.