Inside polyomavirus at 25-A resolution.

J P Griffith; D L Griffith; I Rayment; W T Murakami; D L Caspar

doi:10.1038/355652a0

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Inside polyomavirus at 25-A resolution.

J P Griffith·D L Griffith·I Rayment·W T Murakami·D L Caspar

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Abstract

Empty capsids and complete virions of polyomavirus crystallize isomorphously. Here we use difference Fourier analysis of X-ray diffraction data at 25-A resolution from these crystals to obtain an electron-density map of the inside of the virion. The polyomavirus capsid is built from 72 pentamers of VP1 that form three different types of connections in the T = 7d icosahedral surface lattice. Self-assembly of purified recombinant VP1 into capsid-like aggregates has shown that switching of the bonding specificity to form the unanticipated non-equivalent connections is an inherent property of the VP1 pentamers. Our map of the inside of the virion displays 72 prongs of electron density extending from the core into the axial cavities of the VP1 pentamers. We identify these prongs with the VP2 and VP3 molecules, which may function to guide the assembly of the highly ordered capsid on the nucleohistone core. The atomic structure of the closely related simian virus-40 capsid has been determined from the high-resolution diffraction data. Our polyomavirus map, calculated using all the low-resolution diffraction data, shows no indication of regular order inside the spherical core.

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Capsid Fourier Analysis Polyomavirus Virion X-Ray Diffraction Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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J P Griffith, D L Griffith, I Rayment, W T Murakami, D L Caspar. 1992-02-13. Inside polyomavirus at 25-A resolution.. https://doi.org/10.1038/355652a0

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