| Property | Value |
|---|
|
?:abstract
|
-
A novel coronavirus (SARS-CoV-2) has emerged to a global pandemic and caused significant damages to public health. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides Ang II to control vasodilatation and permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we wonder how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ~3–10 fold when fluorogenic caspase-1 substrate and Bradykinin-analog peptides were used to characterize ACE2 activity. In addition, the enhancement was mediated by ACE2 binding of RBD domain of SARS-CoV-2 spike. These results highlighted the altered activity of ACE2 during SARS-CoV-2 infection and would shed new lights on the pathogenesis of COVID-19 and its complications for better treatments.
|
|
?:creator
|
|
|
?:doi
|
|
|
?:doi
|
-
10.1101/2020.07.01.182659
|
|
?:journal
|
|
|
?:license
|
|
|
?:pdf_json_files
|
-
document_parses/pdf_json/f1fcaaa4f04fe7e7e4e9e19465e681dc78a01c46.json; document_parses/pdf_json/d5a6b2e77235efee6b148aa9b3e0aa33de8e56b7.json
|
|
?:pmc_json_files
|
-
document_parses/pmc_json/PMC7337377.xml.json
|
|
?:pmcid
|
|
|
?:pmid
|
|
|
?:pmid
|
|
|
?:publication_isRelatedTo_Disease
|
|
|
?:sha_id
|
|
|
?:source
|
-
BioRxiv; Medline; PMC; WHO
|
|
?:title
|
-
High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity
|
|
?:type
|
|
|
?:year
|
|
![[This page as RDF]](https://research.tib.eu/covid-19/static/rdf-icon.gif){kind=icon}