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Proteolytic Activation of SARS-CoV-2 Spike at the S1/S2 Boundary: Potential Role of Proteases beyond Furin.
Tang, Tiffany; Jaimes, Javier A; Bidon, Miya K; Straus, Marco R; Daniel, Susan; Whittaker, Gary R.
  • Tang T; Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York 14853, United States.
  • Jaimes JA; Department of Microbiology and Immunology, Cornell University, Ithaca, New York 14853, United States.
  • Bidon MK; Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York 14853, United States.
  • Straus MR; Department of Microbiology and Immunology, Cornell University, Ithaca, New York 14853, United States.
  • Daniel S; Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York 14853, United States.
  • Whittaker GR; Department of Microbiology and Immunology, Cornell University, Ithaca, New York 14853, United States.
ACS Infect Dis ; 7(2): 264-272, 2021 02 12.
Article in English | MEDLINE | ID: covidwho-1023823
Semantic information from SemMedBD (by NLM)
1. Vitronecti AFFECTS C1537068
Subject
Vitronecti
Predicate
AFFECTS
Object
C1537068
2. Cell Count USES Peptide Hydrolases
Subject
Cell Count
Predicate
USES
Object
Peptide Hydrolases
3. Implantation procedure TREATS 2019 novel coronavirus
Subject
Implantation procedure
Predicate
TREATS
Object
2019 novel coronavirus
4. Vitronectin, human AFFECTS Virus Internalization
Subject
Vitronectin, human
Predicate
AFFECTS
Object
Virus Internalization
5. Cell Count USES Peptide Hydrolases
Subject
Cell Count
Predicate
USES
Object
Peptide Hydrolases
6. Implantation procedure TREATS 2019 novel coronavirus
Subject
Implantation procedure
Predicate
TREATS
Object
2019 novel coronavirus
ABSTRACT
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) uses its spike (S) protein to mediate viral entry into host cells. Cleavage of the S protein at the S1/S2 and/or S2' site(s) is associated with viral entry, which can occur at either the cell plasma membrane (early pathway) or the endosomal membrane (late pathway), depending on the cell type. Previous studies show that SARS-CoV-2 has a unique insert at the S1/S2 site that can be cleaved by furin, which appears to expand viral tropism to cells with suitable protease and receptor expression. Here, we utilize viral pseudoparticles and protease inhibitors to study the impact of the S1/S2 cleavage on infectivity. Our results demonstrate that S1/S2 cleavage is essential for early pathway entry into Calu-3 cells, a model lung epithelial cell line, but not for late pathway entry into Vero E6 cells, a model cell line. The S1/S2 cleavage was found to be processed by other proteases beyond furin. Using bioinformatic tools, we also analyze the presence of a furin S1/S2 site in related CoVs and offer thoughts on the origin of the insertion of the furin-like cleavage site in SARS-CoV-2.
Subject(s)
Keywords

Full text: Available Collection: International databases Database: MEDLINE Main subject: Peptide Hydrolases / Furin / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Limits: Animals / Humans Language: English Journal: ACS Infect Dis Year: 2021 Document Type: Article Affiliation country: Acsinfecdis.0c00701

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Peptide Hydrolases / Furin / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Limits: Animals / Humans Language: English Journal: ACS Infect Dis Year: 2021 Document Type: Article Affiliation country: Acsinfecdis.0c00701