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Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS
Michiel van de Waterbeemd1, Aida Llauró2, Joost Snijder1
1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands; Netherlands Proteomics Centre, Utrecht, the Netherlands.
Biophysical Journal
|March 30, 2017
Summary
Minute virus of mice capsid rearrangements distant from pores are key for peptide translocation during infection. Mild heating reveals temperature-dependent dynamics crucial for viral function.
Area of Science:
- Structural biology
- Virology
- Biophysics
Background:
- Icosahedral viral capsids rely on protein subunit dynamics for infection.
- Minute virus of mice (MVM) infection involves peptide translocation through capsid pores, linked to conformational changes.
- Understanding the specific capsid regions involved in these temperature-induced dynamics is crucial.
Purpose of the Study:
- To investigate the temperature-dependent structural dynamics of the minute virus of mice capsid.
- To identify capsid regions involved in the conformational changes associated with peptide translocation.
- To demonstrate the utility of hydrogen-deuterium exchange mass spectrometry (HDX-MS) for studying large protein assemblies.
Main Methods:
- Utilized hydrogen-deuterium exchange coupled with mass spectrometry (HDX-MS).
- Analyzed the dynamics of the MVM capsid across a range of increasing temperatures.
- Correlated observed dynamic changes with known MVM infection mechanisms.
Main Results:
- Temperature-induced peptide translocation involves structural rearrangements in regions remote from the capsid pores.
- Increased dynamics were observed in secondary-structure elements of the capsid shell where spikes emerge.
- Decreased dynamics were noted in the long, intertwined loops forming the large capsid spikes.
- Concluded that MVM translocation involves global capsid rearrangement and complex alterations in equilibrium dynamics.
Conclusions:
- Viral peptide translocation is associated with global capsid rearrangements, not just local pore dynamics.
- HDX-MS is a powerful tool for detailed analysis of temperature-dependent dynamics in large protein assemblies.
- This research provides a foundation for future studies on structure-dynamics-function relationships in viruses and protein cages.