Structural basis of receptor recognition by SARS-CoV-2.
Identifieur interne : 000203 ( 2020/Analysis ); précédent : 000202; suivant : 000204Structural basis of receptor recognition by SARS-CoV-2.
Auteurs : Jian Shang [États-Unis] ; Gang Ye [États-Unis] ; Ke Shi [États-Unis] ; Yushun Wan [États-Unis] ; Chuming Luo [États-Unis] ; Hideki Aihara [États-Unis] ; Qibin Geng [États-Unis] ; Ashley Auerbach [États-Unis] ; Fang Li [États-Unis]Source :
- Nature [ 1476-4687 ] ; 2020.
Abstract
A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-191,2. A key to tackling this pandemic is to understand the receptor recognition mechanism of the virus, which regulates its infectivity, pathogenesis and host range. SARS-CoV-2 and SARS-CoV recognize the same receptor-angiotensin-converting enzyme 2 (ACE2)-in humans3,4. Here we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2. In comparison with the SARS-CoV RBD, an ACE2-binding ridge in SARS-CoV-2 RBD has a more compact conformation; moreover, several residue changes in the SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD-ACE2 interface. These structural features of SARS-CoV-2 RBD increase its ACE2-binding affinity. Additionally, we show that RaTG13, a bat coronavirus that is closely related to SARS-CoV-2, also uses human ACE2 as its receptor. The differences among SARS-CoV-2, SARS-CoV and RaTG13 in ACE2 recognition shed light on the potential animal-to-human transmission of SARS-CoV-2. This study provides guidance for intervention strategies that target receptor recognition by SARS-CoV-2.
DOI: 10.1038/s41586-020-2179-y
PubMed: 32225175
Affiliations:
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wicri:level="2"><nlm:affiliation>Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN</wicri:regionArea><placeName><region type="state">Minnesota</region></placeName></affiliation></author><author><name sortKey="Geng, Qibin" sort="Geng, Qibin" uniqKey="Geng Q" first="Qibin" last="Geng">Qibin Geng</name><affiliation wicri:level="2"><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN</wicri:regionArea><placeName><region type="state">Minnesota</region></placeName></affiliation></author><author><name sortKey="Auerbach, Ashley" sort="Auerbach, Ashley" uniqKey="Auerbach A" first="Ashley" last="Auerbach">Ashley Auerbach</name><affiliation wicri:level="2"><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN</wicri:regionArea><placeName><region type="state">Minnesota</region></placeName></affiliation></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation wicri:level="2"><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN, USA. lifang@umn.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN</wicri:regionArea><placeName><region type="state">Minnesota</region></placeName></affiliation></author></analytic><series><title level="j">Nature</title><idno type="eISSN">1476-4687</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-19<sup>1,2</sup>. A key to tackling this pandemic is to understand the receptor recognition mechanism of the virus, which regulates its infectivity, pathogenesis and host range. SARS-CoV-2 and SARS-CoV recognize the same receptor-angiotensin-converting enzyme 2 (ACE2)-in humans<sup>3,4</sup>. Here we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2. In comparison with the SARS-CoV RBD, an ACE2-binding ridge in SARS-CoV-2 RBD has a more compact conformation; moreover, several residue changes in the SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD-ACE2 interface. These structural features of SARS-CoV-2 RBD increase its ACE2-binding affinity. Additionally, we show that RaTG13, a bat coronavirus that is closely related to SARS-CoV-2, also uses human ACE2 as its receptor. The differences among SARS-CoV-2, SARS-CoV and RaTG13 in ACE2 recognition shed light on the potential animal-to-human transmission of SARS-CoV-2. This study provides guidance for intervention strategies that target receptor recognition by SARS-CoV-2.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Minnesota</li></region></list><tree><country name="États-Unis"><region name="Minnesota"><name sortKey="Shang, Jian" sort="Shang, Jian" uniqKey="Shang J" first="Jian" last="Shang">Jian Shang</name></region><name sortKey="Aihara, Hideki" sort="Aihara, Hideki" uniqKey="Aihara H" first="Hideki" last="Aihara">Hideki Aihara</name><name sortKey="Auerbach, Ashley" sort="Auerbach, Ashley" uniqKey="Auerbach A" first="Ashley" last="Auerbach">Ashley Auerbach</name><name sortKey="Geng, Qibin" sort="Geng, Qibin" uniqKey="Geng Q" first="Qibin" last="Geng">Qibin Geng</name><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><name sortKey="Luo, Chuming" sort="Luo, Chuming" uniqKey="Luo C" first="Chuming" last="Luo">Chuming Luo</name><name sortKey="Shi, Ke" sort="Shi, Ke" uniqKey="Shi K" first="Ke" last="Shi">Ke Shi</name><name sortKey="Wan, Yushun" sort="Wan, Yushun" uniqKey="Wan Y" first="Yushun" last="Wan">Yushun Wan</name><name sortKey="Ye, Gang" sort="Ye, Gang" uniqKey="Ye G" first="Gang" last="Ye">Gang Ye</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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