Nature communications, 2020-04, Vol.11 (1), p.2070-5, Article 2070
2020
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig
- Ist Teil von
- Nature communications, 2020-04, Vol.11 (1), p.2070-5, Article 2070
- Ort / Verlag
- England: Nature Publishing Group
- Erscheinungsjahr
- 2020
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2041-1723eISSN: 2041-1723DOI: 10.1038/s41467-020-16048-4Titel-ID: cdi_doaj_primary_oai_doaj_org_article_3b3d05e197724b28bed5fc76756f4d1d
- Format
- –
- Schlagworte
- ACE2, Angiotensin, Angiotensin-Converting Enzyme 2, Animals, Betacoronavirus - drug effects, Betacoronavirus - metabolism, Binding, Binding, Competitive - drug effects, Catalytic activity, Coronaviridae, Coronaviruses, Cross Reactions, Cross-reactivity, Drug Design, Fusion protein, Humans, Immunoglobulin Fc Fragments - chemistry, Immunoglobulin Fc Fragments - metabolism, Immunoglobulin Fc Fragments - pharmacology, Immunoglobulin G, Immunoglobulin G - chemistry, Immunoglobulin G - metabolism, Immunoglobulin G - pharmacology, Immunoglobulins, In Vitro Techniques, Inhibitory Concentration 50, Membrane Fusion - drug effects, Mice, Mice, Inbred BALB C, Mutation, Neutralization, Neutralization Tests, Peptide Fragments - chemistry, Peptide Fragments - genetics, Peptide Fragments - metabolism, Peptide Fragments - pharmacology, Peptidyl-dipeptidase A, Peptidyl-Dipeptidase A - chemistry, Peptidyl-Dipeptidase A - genetics, Peptidyl-Dipeptidase A - pharmacokinetics, Peptidyl-Dipeptidase A - pharmacology, Prophylaxis, Protein Domains - genetics, Protein Stability, Proteins, Reaction kinetics, Receptors, Receptors, Virus - antagonists & inhibitors, Receptors, Virus - chemistry, Receptors, Virus - genetics, Receptors, Virus - metabolism, Recombinant Fusion Proteins - chemistry, Recombinant Fusion Proteins - genetics, Recombinant Fusion Proteins - pharmacokinetics, Recombinant Fusion Proteins - pharmacology, SARS Virus - drug effects, SARS Virus - metabolism, SARS-CoV-2, Severe acute respiratory syndrome, Severe acute respiratory syndrome coronavirus 2, Spike Glycoprotein, Coronavirus - antagonists & inhibitors, Spike Glycoprotein, Coronavirus - chemistry, Spike Glycoprotein, Coronavirus - metabolism, Spike protein, Vaccines, Viral diseases, Viruses