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Comment
.2020 May 19;52(5):734-736.
doi: 10.1016/j.immuni.2020.04.016. Epub 2020 May 8.

SARS-CoV-2: Combating Coronavirus Emergence

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Comment

SARS-CoV-2: Combating Coronavirus Emergence

Rachel L Graham et al. Immunity..

Abstract

The emergence and rapid global spread of SARS-CoV-2 mark the third such identification of a novel coronavirus capable of causing severe, potentially fatal disease in humans in the 21st century. As noted by Andersen et al. (Nature Medicine), the sequencing of proximal zoonotic ancestors to SARS-CoV-2 has aided in the identification of alleles that may contribute to the virus' virulence in humans.

Copyright © 2020 Elsevier Inc. All rights reserved.

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Figures

Figure 1
Figure 1
Genome Phylogeny and Spike and Receptor-Binding Domain Identity of Representative Group 2b Betacoronaviruses The genome, spike, and RBD sequences of selected group 2b betacoronaviruses were aligned and phylogenetically compared. Sequences were aligned using free end gaps with the Blosum62 cost matrix in Geneious Prime. The phylogenetic tree was constructed from the multiple genome sequence alignment using the neighbor-joining method based on 100 replicates, also in Geneious Prime. The GenBank accession number follows each sequence name. Spike and RBD amino acid sequence identities from their respective alignments are represented by color-coded boxes to the right of each tree position, with colors ranging from yellow (~60% similarity) to purple (~100% similarity), shown in the scale in the lower right. Identities are represented as versus 2003 SARS-CoV spike (listed in figure as “2003 SARS Spike”), versus SARS-CoV-2 spike (“SARS-2 Spike”), versus 2003 SARS-CoV RBD (“2003 SARS RBD”), and versus SARS-CoV-2 RBD (“SARS-2 RBD”). The phylograms and alignments were exported from Geneious and then rendered for publication using EvolView (www.evolgenius.info) and Adobe Illustrator CC 2020.
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Comment on

  • The proximal origin of SARS-CoV-2.
    Andersen KG, Rambaut A, Lipkin WI, Holmes EC, Garry RF.Andersen KG, et al.Nat Med. 2020 Apr;26(4):450-452. doi: 10.1038/s41591-020-0820-9.Nat Med. 2020.PMID:32284615Free PMC article.No abstract available.

References

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    1. Bagdonaite I., Wandall H.H. Global aspects of viral glycosylation. Glycobiology. 2018;28:443–467. - PMC - PubMed
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    1. Li F., Li W., Farzan M., Harrison S.C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science. 2005;309:1864–1868. - PubMed
    1. Nao N., Yamagishi J., Miyamoto H., Igarashi M., Manzoor R., Ohnuma A., Tsuda Y., Furuyama W., Shigeno A., Kajihara M. Genetic Predisposition To Acquire a Polybasic Cleavage Site for Highly Pathogenic Avian Influenza Virus Hemagglutinin. MBio. 2017;8 - PMC - PubMed

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