tetano
Editor, Senior Moderator
Nat Commun. 2020 Apr 24;11(1):2070. doi: 10.1038/s41467-020-16048-4.
Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig.
Lei C[SUP]1,[/SUP][SUP]2[/SUP], Qian K[SUP]1,[/SUP][SUP]2[/SUP], Li T[SUP]1,[/SUP][SUP]2[/SUP], Zhang S[SUP]3[/SUP], Fu W[SUP]4[/SUP], Ding M[SUP]5[/SUP], Hu S[SUP]6,[/SUP][SUP]7[/SUP].
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Abstract
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.
PMID:32332765DOI:10.1038/s41467-020-16048-4
Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig.
Lei C[SUP]1,[/SUP][SUP]2[/SUP], Qian K[SUP]1,[/SUP][SUP]2[/SUP], Li T[SUP]1,[/SUP][SUP]2[/SUP], Zhang S[SUP]3[/SUP], Fu W[SUP]4[/SUP], Ding M[SUP]5[/SUP], Hu S[SUP]6,[/SUP][SUP]7[/SUP].
Author information
Abstract
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.
PMID:32332765DOI:10.1038/s41467-020-16048-4