6 research outputs found
Prevalence of and Factors Related to Tobacco Ban Implementation in Substance Use Disorder Treatment Programs
Behavioral Healthcare Staff Attitudes and Practices Regarding Consumer Tobacco Cessation Services
Effect of HIV-Related Stigma and HIV-Related Stress on HIV Disclosure Concerns: a Study of HIV-Positive Persons on Antiretroviral Therapy at Two Urban Hospitals in Ghana
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
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