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Severe acute respiratory disease in American mink experimentally infected with SARS-CoV-2
Danielle R. Adney, … , Stephanie N. Seifert, Vincent J. Munster
Danielle R. Adney, … , Stephanie N. Seifert, Vincent J. Munster
Published November 22, 2022
Citation Information: JCI Insight. 2022;7(22):e159573. https://doi.org/10.1172/jci.insight.159573.
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Research Article COVID-19

Severe acute respiratory disease in American mink experimentally infected with SARS-CoV-2

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Abstract

An animal model that fully recapitulates severe COVID-19 presentation in humans has been a top priority since the discovery of SARS-CoV-2 in 2019. Although multiple animal models are available for mild to moderate clinical disease, models that develop severe disease are still needed. Mink experimentally infected with SARS-CoV-2 developed severe acute respiratory disease, as evident by clinical respiratory disease, radiological, and histological changes. Virus was detected in nasal, oral, rectal, and fur swabs. Deep sequencing of SARS-CoV-2 from oral swabs and lung tissue samples showed repeated enrichment for a mutation in the gene encoding nonstructural protein 6 in open reading frame 1ab. Together, these data indicate that American mink develop clinical features characteristic of severe COVID-19 and, as such, are uniquely suited to test viral countermeasures.

Authors

Danielle R. Adney, Jamie Lovaglio, Jonathan E. Schulz, Claude Kwe Yinda, Victoria A. Avanzato, Elaine Haddock, Julia R. Port, Myndi G. Holbrook, Patrick W. Hanley, Greg Saturday, Dana Scott, Carl Shaia, Andrew M. Nelson, Jessica R. Spengler, Cassandra Tansey, Caitlin M. Cossaboom, Natalie M. Wendling, Craig Martens, John Easley, Seng Wai Yap, Stephanie N. Seifert, Vincent J. Munster

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Figure 1

Functional SARS-CoV-2 entry analysis with human and mink ACE2.

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Functional SARS-CoV-2 entry analysis with human and mink ACE2.
(A) An aa...
(A) An aa sequence alignment of ACE2 from mink and humans. Residues that participate in the SARS-CoV-2 RBD–ACE2 interaction are noted below the alignment by a blue box. Residues that participate in intermolecular hydrogen bonding or salt bridges are marked with a black dot. ACE2 residues that differ between mink and humans within the interface are outlined with a red box. The substitution at residue 90 affecting an N-linked glycosylation site is noted with a blue box. (B) Differences between mink and human ACE2 are highlighted on the structure of the complex of SARS-CoV-2 RBD in gray bound to human ACE2 in black. Side chains of the ACE2 and RBD residues that participate in the binding interaction are shown as sticks. The mutated residues are indicated by red. (C) SARS-CoV-2 spike pseudotype assay showing relative entry compared with no-spike control in BHK cells expressing human or mink ACE2. Bars depict SD, no significant difference detected between groups by 2-tailed t test.

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