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Structural basis for Fullerene geometry in a human endogenous retrovirus capsid

DOI: 10.1038/s41467-019-13786-y DOI Help

Authors: Oliver Acton (The Francis Crick Institute (MH); University of Washington) , Tim Grant (The Francis Crick Institute; Howard Hughes Medical Institute) , Giuseppe Nicastro (The Francis Crick Institute (Midland Road)) , Neil J. Ball (The Francis Crick Institute) , David C. Goldstone (The Francis Crick Institute; University of Auckland) , Laura E. Robertson (The Francis Crick Institute) , Kasim Sader (The Francis Crick Institute; Thermo Fisher Scientific Materials and Structural Analysis) , Andrea Nans (The Francis Crick Institute) , Andres Ramos (MRC National Institute for Medical Research; University College London) , Jonathan P. Stoye (The Francis Crick Institute; Imperial College London) , Ian A. Taylor (The Francis Crick Institute) , Peter B. Rosenthal (The Francis Crick Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: December 2019
Diamond Proposal Number(s): 13775

Open Access Open Access

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.

Journal Keywords: Cryoelectron microscopy; Solution-state NMR; Viral proteins; X-ray crystallography

Diamond Keywords: Viruses

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography

Added On: 09/01/2020 15:53

Documents:
s41467-019-13786-y.pdf

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Infectious Diseases Pathogens Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)