The amino Acid residues at positions 120 to 123 are crucial for the antigenicity of hepatitis B surface antigen.

ABSTRACT: The major hydrophilic region (MHR) of hepatitis B surface antigen (HBsAg) harbors conformational B-cell epitopes and is the major target of neutralizing antibodies to HBsAg (anti-HBs). Mutant HBsAg (mtHBsAg) with amino acid substitutions such as G145R is known to affect the binding of specific anti-HB antibodies and their detection by conventional diagnostic assays. In the present study, we focused on the role of the amino acid positions 120 to 123, which are around MHR 2 according to the spectrum of recently identified, naturally occurring mtHBsAg. Strikingly, the amino acid substitution K122I abolished the reactivity of HBsAg in all immunoassays tested so far. Also, mtHBsAg G145R could be clearly detected with four different enzyme-linked immunosorbent assays that were based on monoclona

SUBMITTER: Tian Y 

PROVIDER: S-EPMC2045265 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature