Structural basis for Fullerene geometry in a human endogenous retrovirus capsid

Oliver Acton, Tim Grant, Giuseppe Nicastro, Neil J. Ball, David C. Goldstone, Laura E. Robertson, Kasim Sader, Andrea Nans, Andres Ramos, Jonathan P. Stoye, Ian A. Taylor () and Peter B. Rosenthal ()
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Oliver Acton: The Francis Crick Institute
Tim Grant: The Francis Crick Institute
Giuseppe Nicastro: The Francis Crick Institute
Neil J. Ball: The Francis Crick Institute
David C. Goldstone: The Francis Crick Institute
Laura E. Robertson: The Francis Crick Institute
Kasim Sader: The Francis Crick Institute
Andrea Nans: The Francis Crick Institute
Andres Ramos: MRC National Institute for Medical Research
Jonathan P. Stoye: The Francis Crick Institute
Ian A. Taylor: The Francis Crick Institute
Peter B. Rosenthal: The Francis Crick Institute

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract The HML2 (HERV-K) group constitutes the most recently acquired family of human endogenous retroviruses, with many proviruses less than one million years old. Many maintain intact open reading frames and provirus expression together with HML2 particle formation are observed in early stage human embryo development and are associated with pluripotency as well as inflammatory disease, cancers and HIV-1 infection. Here, we reconstruct the core structural protein (CA) of an HML2 retrovirus, assemble particles in vitro and employ single particle cryogenic electron microscopy (cryo-EM) to determine structures of four classes of CA Fullerene shell assemblies. These icosahedral and capsular assemblies reveal at high-resolution the molecular interactions that allow CA to form both pentamers and hexamers and show how invariant pentamers and structurally plastic hexamers associate to form the unique polyhedral structures found in retroviral cores.

Date: 2019
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DOI: 10.1038/s41467-019-13786-y

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