期刊
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
卷 406, 期 5, 页码 1437-1446出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-013-7548-z
关键词
Native MS; GEMMA; Hepatitis B; Virus-antibody complexes; Quasi-equivalence; Immune complex
资金
- Netherlands Organization for Scientific Research (NWO)
- ALW-ECHO [819.02.10]
- Netherlands Proteomics Centre, embedded in the Netherlands Genomics Initiative
- Austrian Science Foundation [TRP 29-N20]
- Intramural Research Program of the National Institute of Arthritis and Musculoskeletal and Skin Diseases at the National Institutes of Health
The capsid of hepatitis B virus (HBV) is a major viral antigen and important diagnostic indicator. HBV capsids have prominent protrusions ('spikes') on their surface and are unique in having either T = 3 or T = 4 icosahedral symmetry. Mouse monoclonal and also human polyclonal antibodies bind either near the spike apices (historically the 'alpha-determinant') or in the 'floor' regions between them (the 'beta-determinant'). Native mass spectrometry (MS) and gas-phase electrophoretic mobility molecular analysis (GEMMA) were used to monitor the titration of HBV capsids with the antigen-binding domain (Fab) of mAb 3120, which has long defined the beta-determinant. Both methods readily distinguished Fab binding to the two capsid morphologies and could provide accurate masses and dimensions for these large immune complexes, which range up to similar to 8 MDa. As such, native MS and GEMMA provide valuable alternatives to a more time-consuming cryo-electron microscopy analysis for preliminary characterisation of virus-antibody complexes.
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