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Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
DOI:
10.1038/s41467-019-13786-y
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
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:
Pathogens
Infectious Diseases
Health & Wellbeing
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)