Maturation Dynamics of a Viral Capsid Visualization of Transitional Intermediate States

Abstract

Typical of DNA bacteriophages and herpesviruses, HK97 assembles in two stages: polymerization and maturation. First, capsid protein polymerizes into closed shells; then, these precursors mature into larger, stabler particles. Maturation is initiated by proteolysis, producing a metastable particle primed for expansion-the major structural transition. We induced expansion in vitro by acidic pH and monitored the resulting changes by time-resolved X-ray diffraction and cryo-electron microscopy. The transition, which is not synchronized over the population, proceeds in a series of stochastically triggered subtransitions. Three distinct intermediates were identified, which are comparable to transitional states in protein folding. The intermediates' structures reveal the molecular events occurring during expansion. Integrated into a movie (see Dynamic Visualization below), they show capsid maturation as a dynamic process.

DOI: 10.1016/S0092-8674(00)81563-9

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@article{Lata2000MaturationDO, title={Maturation Dynamics of a Viral Capsid Visualization of Transitional Intermediate States}, author={Ramani Lata and James F Conway and Naiqian Cheng and Robert L. Duda and Roger W. Hendrix and William R . Wikoff and John E. Johnson and Hiro Tsuruta and Alasdair C. Steven}, journal={Cell}, year={2000}, volume={100}, pages={253-263} }