| Literature DB >> 33432184 |
Cornelia Blume1,2, Claire L Jackson1,2,3, Cosma Mirella Spalluto1,4, Jelmer Legebeke5, Liliya Nazlamova1, Franco Conforti1,2, Jeanne-Marie Perotin2,6, Martin Frank7, John Butler8, Max Crispin3,8, Janice Coles1,2, James Thompson1,2, Robert A Ridley1,2, Lareb S N Dean1,2, Matthew Loxham1,2,3, Stephanie Reikine9, Adnan Azim1,2, Kamran Tariq1,2, David A Johnston1,10, Paul J Skipp3,8, Ratko Djukanovic1,2, Diana Baralle2,5, Christopher J McCormick1,2, Donna E Davies11,12,13, Jane S Lucas14,15,16, Gabrielle Wheway17,18, Vito Mennella19,20,21.
Abstract
Angiotensin-converting enzyme 2 (ACE2) is the main entry point in airway epithelial cells for SARS-CoV-2. ACE2 binding to the SARS-CoV-2 protein spike triggers viral fusion with the cell plasma membrane, resulting in viral RNA genome delivery into the host. Despite ACE2's critical role in SARS-CoV-2 infection, full understanding of ACE2 expression, including in response to viral infection, remains unclear. ACE2 was thought to encode five transcripts and one protein of 805 amino acids. In the present study, we identify a novel short isoform of ACE2 expressed in the airway epithelium, the main site of SARS-CoV-2 infection. Short ACE2 is substantially upregulated in response to interferon stimulation and rhinovirus infection, but not SARS-CoV-2 infection. This short isoform lacks SARS-CoV-2 spike high-affinity binding sites and, altogether, our data are consistent with a model where short ACE2 is unlikely to directly contribute to host susceptibility to SARS-CoV-2 infection.Entities:
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Year: 2021 PMID： 33432184 DOI： 10.1038/s41588-020-00759-x
Source DB: PubMed Journal: Nat Genet ISSN： 1061-4036 Impact factor: 41.307