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Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography

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Science  04 Jun 2015:
aaa5182
DOI: 10.1126/science.aaa5182

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Abstract

Retroviruses depend upon self-assembly of their capsid proteins (core particle) to yield infectious mature virions. Despite the essential role of the retroviral core, its high polymorphism has hindered high-resolution structural analyses. Here, we report the x-ray structure of the native capsid (CA) protein from bovine leukemia virus. CA is organized as hexamers that deviate significantly from 6-fold symmetry, yet adjust to make two-dimensional pseudo-hexagonal arrays that mimic mature retroviral cores. Intra- and interhexameric quasi-equivalent contacts are uncovered, with flexible trimeric lateral contacts among hexamers, yet preserving very similar dimeric interfaces making the lattice. The conformation of each capsid subunit in the hexamer is therefore dictated by long-range interactions, revealing how the hexamers can also assemble into closed core particles, a relevant feature of retrovirus biology.

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