Nature Structural Biology10, 334 - 341 (2003)
Published online: 21 April 2003; | doi:10.1038/nsb922
Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
J. Bernard Heymann1, Naiqian Cheng1, William W. Newcomb2, Benes L. Trus1, 3, Jay C. Brown2
& Alasdair C. Steven1
1
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892.
2
Department of Microbiology, University of Virginia Health System, Charlottesville, Virginia 22908.
3
Imaging Sciences Laboratory, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892.
The capsid of the herpes simplex virus initially assembles as a procapsid that matures through a massive conformational change of its 182 MDa surface shell. This transition, which stabilizes the fragile procapsid, is facilitated by the viral protease that releases the interaction between the shell and the underlying scaffold; however, protease-deficient procapsids mature slowly in vitro. To study procapsid maturation as a time-resolved process, we monitored this reaction by cryo-electron microscopy (cryo-EM). The resulting images were sorted into 17 distinct classes, and three-dimensional density maps were calculated for each. When arranged in a chronological series, these maps yielded molecular movies of procapsid maturation. A single major switching event takes place at stages 8−9, preceded by relatively subtle adjustments in the pattern of interactions and followed by similarly small 'aftershocks'. The primary mechanism underlying maturation is relative rotations of domains of VP5, the major capsid protein.
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