Antigenic and physicochemical characterization of the 2nd International Standard for hepatitis B virus surface antigen (HBsAg)
| Autor: | Wolfram H. Gerlich, Ulrike C. Wend, Fabian M. Faupel, Christian G. Schüttler, P. Nico Lelie |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
HBsAg
Antigenicity Biology medicine.disease_cause Virus Antigen Orthohepadnavirus Virology medicine Animals Humans Polyacrylamide gel electrophoresis Immunoassay Hepatitis B virus Hepatitis B Surface Antigens virus diseases Reference Standards Hepatitis B biology.organism_classification Molecular biology digestive system diseases Infectious Diseases Hepadnaviridae Chromatography Gel Electrophoresis Polyacrylamide Gel Ultracentrifugation |
| Zdroj: | Journal of Clinical Virology. 47:238-242 |
| ISSN: | 1386-6532 |
| Popis: | Background: Standard preparations for HBsAg are required for quality control of test kits and clinical studies on HBsAg quantitation. WHO provides purified heat inactivated HBsAg diluted in negative defribinated plasma as 2nd International Standard (IS) for quality control of tests. Objective: Study of possible alterations of antigenicity, protein composition, size and density of the heat inactivated source material (SM) for the 2nd IS. Study design: Native HBsAg and SM were examined by quantitative immune electrophoresis (QIE), SDS-PAGE, ultracentrifugation and gel chromatography. HBV DNA was sequenced and the HBsAg geno/subtype derived. Results: The SM contained 97,600 International Units HBsAg/ml in QIE which agreed very well with the previous evaluations by WHO using 10 different assays. In SDS-PAGE, SM showed on a strong background the small HBs proteins but no preS proteins. SM had a more heterogeneous density than native HBsAg and contained particle aggregates. The HBsAg geno/subtype of SM was A2/adw2. Conclusions: The IS has very good HBs antigenicity, but it lacks the preS domains, has modified HBs proteins and is partially aggregated. While it has been proven very useful for quality control of tests, certain inconsistencies due to the altered structure of its HBsAg cannot be excluded. |
| Databáze: | OpenAIRE |
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