Effect of variation in the common 'a' determinant on the antigenicity of hepatitis B surface antigen
| Autor: | Beatus Ofenloch, Howard C. Thomas, Peter Karayiannis, Andrea Horsch, Jennifer A. Waters, Ralph Gehrke, Georg Hess, Sarah Jeffers, Siamak Seddigh-Tonekaboni |
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| Rok vydání: | 1999 |
| Předmět: |
Antigenicity
HBsAg Hepatitis B virus Silver Staining Genetic Vectors Molecular Sequence Data Molecular Probe Techniques medicine.disease_cause Polymerase Chain Reaction Epitope Pichia Epitopes Antigen Virology medicine Antigenic variation Humans Amino Acid Sequence Cloning Molecular Child In Situ Hybridization Hepatitis B Surface Antigens biology biology.organism_classification Antigenic Variation Recombinant Proteins Infectious Diseases Hepadnaviridae Amino Acid Substitution Child Preschool biology.protein Mutagenesis Site-Directed Antibody Epitope Mapping |
| Zdroj: | Journal of medical virology. 60(2) |
| ISSN: | 0146-6615 |
| Popis: | Antibody to the common “a” determinant of hepatitis B surface antigen (HBsAg) protects against infection with hepatitis B virus. A number of variant surface antigens with amino acid substitutions within the “a” determinant have been described in patients around the world. Both wild type and variant HBsAgs were expressed in the yeast Pichia pastoris and the antigens were semi-purified and quantitated. The effect on antigenicity of these changes was investigated in a quantitative fashion using four monoclonal antibodies known to bind to different epitopes within the common “a” determinant. The results suggest that amino acid substitution of T131I, K141E and G145R and insertion of 3 amino acids between residues 123 and 124 markedly affect the antigenic structure of HBsAg. These substitutions and insertions in the viral envelope may lead to evasion of the virus neutralizing antibody response and also to reduce efficiency of detection by immunoassays used for diagnosis and blood-bank screening. J. Med. Virol. 60:113–121, 2000. © 2000 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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