Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2.
Cell
; 181(4): 894-904.e9, 2020 05 14.
Article
in English
| MEDLINE | ID: covidwho-45975
ABSTRACT
The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Peptidyl-Dipeptidase A
/
Virus Internalization
/
Spike Glycoprotein, Coronavirus
/
Betacoronavirus
Type of study:
Randomized controlled trials
Limits:
Humans
Language:
English
Journal:
Cell
Year:
2020
Document Type:
Article
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