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Review
. 2011 Apr;21(2):265-73.
doi: 10.1016/j.sbi.2011.01.008. Epub 2011 Feb 18.

Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy

Nikolaus Grigorieff  1 , Stephen C Harrison
Affiliations
Review

Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy

Nikolaus Grigorieff et al. Curr Opin Struct Biol. 2011 Apr.

Abstract

Nine different near-atomic resolution structures of icosahedral viruses, determined by electron cryo-microscopy and published between early 2008 and late 2010, fulfil predictions made 15 years ago that single-particle cryo-EM techniques could visualize molecular detail at 3-4Å resolution. This review summarizes technical developments, both in instrumentation and in computation, that have led to the new structures, which advance our understanding of virus assembly and cell entry.

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Figures

Fig. 1
Fig. 1
Comparison of x-ray crystallographic and EM density maps of the rotavirus DLP [1]. (a) X-ray crystallographic 2Fo-Fc density map, filtered to 4.2 Å resolution, with refined atomic model superimposed [59]. The residue numbering refers to the VP6 polypeptide chain. (b) Same area as in (a) but showing the cryo-EM map. Modified from [1].
Fig. 2
Fig. 2
3D reconstruction of adenovirus type 5 [8]. The overall diameter of the particle (not including the spikes) is about 900 Å. Superposed on a surface rendering are triangles highlighting the hexon subunits. Polypeptide chains of one of the arm-like "cement" proteins (protein IX), shown as colored "worms", winds between hexons on the external surface of the particle. The other cement proteins are on the interior of the hexon shell; their locations are symbolized by magenta (protein IIIa) and orange (protein VIII) bars. Modified from [69].
See this image and copyright information in PMC

References

    1. Zhang X, Settembre E, Xu C, Dormitzer PR, Bellamy R, Harrison SC, Grigorieff N. Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction. Proc Natl Acad Sci U S A. 2008;105:1867–1872. Reports a 3.8 Å resolution map of the rotavirus double-layered particle, validated in molecular detail by comparison with a crystal structure of the same particle.

    1. Jiang W, Baker ML, Jakana J, Weigele PR, King J, Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature. 2008;451:1130–1134. Reports a 4.5 Å resolution map of bacteriophage ε15. Two proteins make up a heterodimeric protomer in the T=7 icosahedral surface lattice. The secondary structure and approximate chain trace of one of the two proteins establishes its homology with the coat protein of bacteriophage HK97.

    1. Yu X, Jin L, Zhou ZH. 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature. 2008;453:415–419. Reports a 3.9 Å resolution map of cytoplasmic polyhedrosis virus, with a de novo polypeptide chain tracing of the component proteins.

    1. Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N. Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc Natl Acad Sci U S A. 2009;106:10644–10648. Reports a structure at 4.2 Å resolution of a VP7-recoated, rotavirus double-layered particle (DLP) and shows how trimers of VP7, one of the two viral outer-layer proteins, fit onto trimers of VP6, the DLP structural component arrayed in a T=13 l icosahedral lattice.

    1. Wolf M, Garcea RL, Grigorieff N, Harrison SC. Subunit interactions in bovine papillomavirus. Proc Natl Acad Sci U S A. 2010;107:6298–6303. A 3.6 Å resolution map of a bovine papillomavirus particle yields a complete atomic model of the 72-pentamer icosahedral shell, allowing refinement of coordinates (R=37.7%, 15-3.6 Å). The structure corrects and extends an earlier model for key interactions in papillomavirus particle assembly.

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