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Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsids
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Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsids
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Journal Article
Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsids
2014
Overview
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 ‘α-determinant’) or in the ‘floor’ regions between them (the ‘β-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 β-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 ~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.
Figure
Monitoring the binding of the antigen-binding domain (Fab) of mAb 3120 to hepatitis B capsids by native MS and GEMMA
Publisher
Springer Berlin Heidelberg,Springer,Springer Nature B.V
Subject
/ Antigen-Antibody Complex - chemistry
/ Antigens
/ Antigens, Viral - immunology
/ capsid
/ Characterization and Evaluation of Materials
/ Chemistry and Materials Science
/ Hepatitis B virus - chemistry
/ Hepatitis B virus - immunology
/ Humans
/ Immunoglobulin Fab Fragments - chemistry
/ Methods
/ mice
/ Monitoring/Environmental Analysis
/ Protein Interaction Domains and Motifs
/ Proteins
/ Spectrometry, Mass, Electrospray Ionization - methods
/ Viruses
/ Yeast
