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Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig #MMPMID32332765
Lei C; Qian K; Li T; Zhang S; Fu W; Ding M; Hu S
Nat Commun 2020[Apr]; 11 (1): 2070 PMID32332765show ga
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) emerged in Wuhan, China, at the end of 2019, and there are currently no specific antiviral treatments or vaccines available. SARS-CoV-2 has been shown to use the same cell entry receptor as SARS-CoV, angiotensin-converting enzyme 2 (ACE2). In this report, we generate a recombinant protein by connecting the extracellular domain of human ACE2 to the Fc region of the human immunoglobulin IgG1. A fusion protein containing an ACE2 mutant with low catalytic activity is also used in this study. The fusion proteins are then characterized. Both fusion proteins have a high binding affinity for the receptor-binding domains of SARS-CoV and SARS-CoV-2 and exhibit desirable pharmacological properties in mice. Moreover, the fusion proteins neutralize virus pseudotyped with SARS-CoV or SARS-CoV-2 spike proteins in vitro. As these fusion proteins exhibit cross-reactivity against coronaviruses, they have potential applications in the diagnosis, prophylaxis, and treatment of SARS-CoV-2.
|*Neutralization Tests[MESH]
|Angiotensin-Converting Enzyme 2[MESH]
|Animals[MESH]
|Betacoronavirus/*drug effects/metabolism[MESH]
|Binding, Competitive/drug effects[MESH]
|Cross Reactions[MESH]
|Drug Design[MESH]
|Humans[MESH]
|Immunoglobulin Fc Fragments/*chemistry/metabolism/pharmacology[MESH]