Receptor-binding loops in alphacoronavirus adaptation and evolution

Alan H. M. Wong; Aidan C. A. Tomlinson; Dongxia Zhou; Malathy Satkunarajah; Kevin Chen; Chetna Sharon; Marc Desforges; Pierre J. Talbot; James M. Rini

doi:10.1038/s41467-017-01706-x

Nature Communications (Nov 2017)

Receptor-binding loops in alphacoronavirus adaptation and evolution

Alan H. M. Wong,
Aidan C. A. Tomlinson,
Dongxia Zhou,
Malathy Satkunarajah,
Kevin Chen,
Chetna Sharon,
Marc Desforges,
Pierre J. Talbot,
James M. Rini

Affiliations

Alan H. M. Wong: Department of Biochemistry, University of Toronto
Aidan C. A. Tomlinson: Department of Biochemistry, University of Toronto
Dongxia Zhou: Department of Molecular Genetics, University of Toronto
Malathy Satkunarajah: Department of Molecular Genetics, University of Toronto
Kevin Chen: Department of Biochemistry, University of Toronto
Chetna Sharon: Department of Molecular Genetics, University of Toronto
Marc Desforges: Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Institut National de la Recherche Scientifique, Université du Québec
Pierre J. Talbot: Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Institut National de la Recherche Scientifique, Université du Québec
James M. Rini: Department of Biochemistry, University of Toronto

DOI: https://doi.org/10.1038/s41467-017-01706-x
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 10

Abstract

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Coronaviruses have a relatively high mutation rate, potentially allowing fast adaptation to changing pressures. Here, Wong et al. provide the structure of the receptor-binding domain (RBD) of the human coronavirus HCoV-229E and its receptor and analyze the evolution of the RBD over the past 50 years.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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