2020 Abstract:
Cell entry mechanisms of SARS-CoV-2
Abstract: A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) is causing the global coronavirus disease 2019 (COVID-19) pandemic. Understanding how SARS-CoV-2 enters human cells is a high priority for deciphering its mystery and curbing its spread. A virus surface spike protein mediates SARS-CoV-2 entry into cells. To fulfill its function, SARS-CoV-2 spike binds to its receptor human ACE2 (hACE2) through its receptor-binding domain (RBD) and is proteolytically activated by human protea…
Search citation statements
Paper Sections
Select...
2,120
1,189
307
182
Citation Types
70
3,682
5
58
Year Published
2019
2026
Publication Types
Select...
2,646
577
169
103
Relationship
13
3,482
Authors
Journals
Cited by 3,460 publications
(3,817 citation statements)
References 49 publications
70
3,682
5
58
“…S4E). These results are consistent with previous reports (Hoffmann et al, 2020;Shang et al, 2020) and ensure the proper entry mode of the pseudoviruses produced in this study.…”
Section: Resultssupporting
confidence: 94%
“…S4E). These results are consistent with previous reports (Hoffmann et al, 2020;Shang et al, 2020) and ensure the proper entry mode of the pseudoviruses produced in this study.…”
Section: Resultssupporting
confidence: 94%
“…Together, the data suggest a modest role for Spike-protein glycosylation on direct Spike-ACE2 binding. Our observation that the binding of RBD for ACE2 was substantially higher than S1-ACE2 interactions is consistent with a previous report ( Shang et al, 2020 ). This highlights the need to carefully consider RBD presentation/conformation in the context of the full protein when quantifying molecular affinity to ACE2.…”
Section: Resultssupporting
confidence: 94%
“…When comparing S priming by TMPRSS2 during pseudovirus production to priming during entry into target cells, we found that co-expressing TMPRSS2 during pseudovirus production reduced pseudovirus infectivity, possibly due to TMPRSS2-induced premature activation of S that promotes conformational changes to fusion-incompetent or post-fusion structures ( Fig 1C ). This finding is consistent with a previous report suggesting the importance of tight regulation of protease cleavage of the S protein for preserving SARS-CoV-2 infectivity [ 56 ].…”
Section: Resultssupporting
confidence: 94%
