It has been well established that the hepatitis B virus (HBV) surface antigen has three components: the S protein (major protein), the M protein, and the L protein. Hepatitis B surface antigen (HBsAg) particles are mainly composed of 226 amino acid glycoproteins, of which the S protein is the most abundant and encoded by the S gene. This glycoprotein has an important B cell epitope that induces protective antibody responses. It is a kind of transmembrane protein with an N-terminal (TM1), the central (TM2), and a hydrophobic C-terminal domain (HCR) across a membrane structure. S protein monomers aggregate in the endoplasmic reticulum and are secreted into plasma from the host cell as pseudoparticles. The transmembranous S protein(s) has an important role in virus assembly and stabilizes the viral envelope as a dimeric form. Regions of S protein residues between 120 and 150 exposed to the surface of HBV particles represent all HBV α determinants. Common anti-α antibodies were isolated, which protected adults against most infections.
Fig.1 High load of HBsAg suppresses innate and adaptive immune responses through different mechanisms.1
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