Mass spectrometry-based studies of virus assembly.

The assembly of exact numbers of protein monomers into the distinct architectures of virus capsids has long been of intrigue. Despite the diseases associated with viruses, there is a paucity of anti-viral therapies; however, mapping virus capsid assembly at the molecular level may lead to the development of more therapeutics. Native mass spectrometry is a powerful, versatile tool with which to monitor biomolecular assembly pathways and identify key intermediates. Recent highlights in this field in terms of MDa mass measurements, identification of capsid intermediates, and the effect of external parameters on assembly are discussed. Examples from ion mobility spectrometry-mass spectrometry, charge detection mass spectrometry, and gas-phase electrophoretic molecular analysis research are presented.