The structure of a plant-specific partitivirus capsid reveals a unique coat protein domain architecture with an intrinsically disordered protrusion

Matthew Byrne; Aseem Kashyap; Lygie Esquirol; Neil Ranson; Frank Sainsbury

doi:10.1038/s42003-021-02687-w

Communications Biology (Oct 2021)

The structure of a plant-specific partitivirus capsid reveals a unique coat protein domain architecture with an intrinsically disordered protrusion

Matthew Byrne,
Aseem Kashyap,
Lygie Esquirol,
Neil Ranson,
Frank Sainsbury

Affiliations

Matthew Byrne: Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds
Aseem Kashyap: Centre for Cell Factories and Biopolymers, Griffith Institute for Drug Discovery, Griffith University
Lygie Esquirol: Centre for Cell Factories and Biopolymers, Griffith Institute for Drug Discovery, Griffith University
Neil Ranson: Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds
Frank Sainsbury: Centre for Cell Factories and Biopolymers, Griffith Institute for Drug Discovery, Griffith University

DOI: https://doi.org/10.1038/s42003-021-02687-w
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 8

Abstract

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Byrne et al determine the structure of Pepper cryptic virus 1 by Cryo-EM. They identify a disordered region that forms the outermost portion of the deltapartitivirus capsid protrusion that is characteristic of the plant-specific genus.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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