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From chemistry and physics to biology

Icosahedral virus structures

Nature volume 511, pages 16–17 (2014)Cite this article

The early 1980s marked the expansion of crystallographic analysis from organic materials and isolated proteins to more complex biological samples. The first crystal structures of plant RNA viruses revealed the inherent symmetry of viral capsid assemblies, and the subsequent elucidation of a surface antigen of influenza virus provided the first structure of pathological relevance.

Two years later, Abad-Zapatero and colleagues solved the crystal structure of the southern bean mosaic virus (SBMV) capsid. The capsid was found to share the same quasi-equivalent arrangement of protein subunits in the viral shell as TBSV, despite the absence of one of the two domains of the TBSV coat protein, and a β-annulus structure was again formed by interactions of the ordered N-terminal structures of one third of the constituent subunits. Together, the symmetric arrangement of hexamers and pentamers within these two capsid structures exemplified the “quasi-equivalence” theory of Caspar and Klug, which predicted that icosahedral symmetry could be achieved through identical protein subunits whose specific interactions are determined by their position within the viral capsid.

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References

ORIGINAL RESEARCH PAPERS

  1. Harrison, S. C. et al. Tomato bushy stunt virus at 2.9 Å resolution. Nature 276, 368–373 (1978)

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  2. Abad-Zapatero, C. et al. Structure of southern bean mosaic virus at 2.8 Å resolution. Nature 286, 33–39 (1980)

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  3. Wilson, I. A., Skehel, J. J. & Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366–373 (1981)

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FURTHER READING

  1. Caspar, D. L. D. & Klug, A. Physical principles in the construction of regular viruses. Cold Spring Harbor Symp. 27, 1–24 (1962)

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  1. Associate Editor, Nature Structural & Molecular Biology,

    Beth Moorefield

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  1. Beth Moorefield
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Moorefield, B. From chemistry and physics to biology. Nature 511 (Suppl 7509), 16–17 (2014). https://doi.org/10.1038/nature13365

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