Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS.

ABSTRACT: Icosahedral viral capsids are made of a large number of symmetrically organized protein subunits whose local movements can be essential for infection. In the capsid of the minute virus of mice, events required for infection that involve translocation of peptides through capsid pores are associated with a subtle conformational change. In vitro, this change can be reversibly induced by overcoming the energy barrier through mild heating of the capsid, but little is known about the capsid regions involved in the process. Here, we use hydrogen-deuterium exchange coupled to mass spectrometry to analyze the dynamics of the minute virus of mice capsid at increasing temperatures. Our results indicate that the transition associated with peptide translocation involves the structural rearrangement of

SUBMITTER: van de Waterbeemd M 

PROVIDER: S-EPMC5375139 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature