Fine-mapping of the B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen

In this study, we report the exact localization and substitutional characterization of a B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen. A set of deletion variants containing preS2 sequences of different length was generated on the basis of frCP as a c...

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Bibliographic Details
Published in:Journal of immunological methods 2002-02, Vol.260 (1), p.251-261
Main Authors: Sominskaya, Irina, Paulij, Wilma, Jansons, Juris, Sobotta, Dirk, Dreilina, Dzidra, Sunnen, Cecile, Meisel, Helga, Gerlich, Wolfram H, Pumpens, Paul
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies, Monoclonal - immunology
Biological and medical sciences
Blotting, Western
Epitope Mapping
Epitopes, B-Lymphocyte - analysis
Epitopes, B-Lymphocyte - genetics
Epitopes, B-Lymphocyte - immunology
Fundamental and applied biological sciences. Psychology
Fundamental immunology
hepatitis B surface antigen
Hepatitis B Surface Antigens - analysis
Hepatitis B Surface Antigens - genetics
Hepatitis B Surface Antigens - immunology
Hepatitis B virus
Human viral diseases
Infectious diseases
Medical sciences
Mice
Microbiology
Molecular immunology
Molecular Sequence Data
Monoclonal antibody
preS2 domain
Protein Precursors - analysis
Protein Precursors - genetics
Protein Precursors - immunology
Techniques
Viral diseases
Viral Envelope Proteins - genetics
Viral Envelope Proteins - immunology
Viral hepatitis
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Summary:In this study, we report the exact localization and substitutional characterization of a B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen. A set of deletion variants containing preS2 sequences of different length was generated on the basis of frCP as a carrier. It was found after Western blot analysis that three monoclonal antibodies (MAbs) (2-11B1, 3-11C2, HB.OT10) recognized the linear preS2 sequence within the amino acid (aa) stretch 3-WNSTTFHQTLQDP-13. The importance of each aa residue of the epitope was proved by comparison of antibody binding to alanine-substituted peptides in both free-peptide and Pepscan variants.
ISSN:0022-1759
1872-7905
DOI:10.1016/S0022-1759(01)00551-8