Antibody responses to recombinant and plasma derived hepatitis B vaccines.

Abstract

The antibody response to hepatitis B surface antigen (anti-HBs) induced in 25 recipients of a recombinant hepatitis B vaccine derived from yeast was compared with that induced in 25 recipients of a vaccine prepared from hepatitis B surface antigen (HBsAg) derived from plasma. Anti-HBs affinity and specificity were compared using assays of antibody affinity with two different antigens, a complex of the major polypeptide of HBsAg (p25; molecular weight 25000 daltons) covalently linked to its glycosylated form (gp3O) prepared from native purified HBsAg, and a cyclical synthetic peptide representing amino acid residues 139-147 of the major polypeptide of HBsAg and known to represent a major part of an a determinant. There was no difference in anti-HBs affinity or molar antigen binding sites of the antibody measured with either antigen between the two groups. All subjects in both groups produced antibody that bound to the gp3O/p25 complex antigen, whereas 22 of the recipients of the plasma derived vaccine compared with 24 of those receiving the yeast derived vaccine produced antibodies that bound to the cyclical synthetic peptide 139-147. These results support the finding of similar levels of anti-HBs, measured by commercial solid phase radioimmunoassay, in the two vaccine groups after three doses of vaccine.These results show no significant difference in the quantity, quality, or specificity of the anti-HBs response induced by the recombinant hepatitis B vaccine and the plasma derived hepatitis B vaccine.

Preparation and Properties of Immune-stimulating Complexes Containing Hepatitis B Virus Surface Antigen

“…These observations indicate that this peptide represents the dominant epitope of HBsAg to which protective antibodies are directed, and that the measurement of antibody binding to C139 is a useful procedure for the evaluation of sera positive for anti-HBs. In the present study, mice immunized with an iscom preparation of the p25 HBsAg polypeptide produced antibody which bound to the C 139 peptide (Table 2) with an affinity similar to that measured previously in human and animal sera containing antibodies to hepatitis B vaccines (Brown et al, 1984(Brown et al, , 1986. The highest affinity values were obtained with animals in the group receiving 0.2 p~g of the iscom preparation, although the response was short-lived in this group.…”

“…wt. HBsAg polypeptides is bound with high affinity by a major proportion of specific antibodies to HBsAg in the sera of healthy persons immunized either with the currently licensed hepatitis B vaccine (Brown et al, 1984) or with a yeast-derived recombinant hepatitis B vaccine (Brown et al, 1986). These observations indicate that this peptide represents the dominant epitope of HBsAg to which protective antibodies are directed, and that the measurement of antibody binding to C139 is a useful procedure for the evaluation of sera positive for anti-HBs.…”

Hepatitis B virus S mutants in liver transplant recipients who were reinfected despite hepatitis B immune globulin prophylaxis

“…5,6 This region is conformational and is thought to consist of two loops held by disulfide bridges between cysteines 124 and 137, and cysteines 138 and 147. 7 The second loop is more conserved and confers most of the antigenicity of the 'a' determinant; this loop is sometimes referred to as the major hydrophilic region (MHR).…”

Hepatitis B Surface Gene Mutants and their Emerging Role in the Efficacy of HBV Vaccination Programs

“…This area is highly immunogenic and forms the basis of HBsAg vaccines. The major B cell epitopes of HBsAg have been shown to reside in the a determinant at amino acid positions 139-147, 15,16 and elicit anti-HBs capable of cross-protection among the different subtypes. However, selective pressures, such as anti-HBs response as a result of immunization or administration of monoclonal antibodies during prophylaxis, are capable of inducing an environment that may encourage "escape mutants" to emerge.…”