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Determination of the Protective Effects of Neutralizing Anti‐Hepatitis B Virus (HBV) Immunoglobulins by Epitope Mapping with Recombinant HBV Surface‐Antigen Proteins
Author(s) -
Park Junghyun,
Cho Eunwie,
Lee Yunjung,
Shin Song Yub,
Kim Kil Lyong
Publication year - 2000
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2000.tb02552.x
Subject(s) - epitope , virology , antibody , antigen , hepatitis b virus , biology , recombinant dna , hepatitis b , virus , epitope mapping , immunology , biochemistry , gene
Anti‐hepatitis B virus (HBV) surface‐antigen immunoglobulins prepared from human sera are clinical reagents which have been approved for prophylactic treatment in HBV‐exposed persons. The passive immunoprophylaxis with immunoglobulins is meant to cross‐link viral particles, which are then further cleared by the host's own immune system. While antibodies specific for both anti‐S‐ and anti‐preS proteins have been proved to serve as effective anti‐viral agents, so far the fine antigen specificity of clinical immunoglobulin preparations has not been determined. Using recombinant proteins covering the hepatitis B surface antigen, in the present study, the specificity of a commercially available immunoglobulin preparation was determined and immunodominant epitopes were mapped. Here, it is shown that the major reactivity of anti‐HBV immunoglobulins is directed against the S‐protein, and that no reactivity to the preS2 but a weak binding activity to the preS1 region was detectable. The antigen reactivity within the preS1 region was biased to the C‐terminal region, which indicates the presence of a putative B‐cell epitope. The evaluation of the antigen specificity and determination of novel protective epitopes will provide valuable information for the further development and improvement of prophylactic HBV immunoglobulins.