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Details on Person In a SARS-CoV-2 infection the cellular protease furin cleave...
| Class:Id | Summation:9770216 |
|---|---|
| _displayName | In a SARS-CoV-2 infection the cellular protease furin cleave... |
| _timestamp | 2022-04-04 08:37:13 |
| created | [InstanceEdit:9770215] Stephan, Ralf, 2022-03-26 |
| modified | [InstanceEdit:9770327] Stephan, Ralf, 2022-04-04 [InstanceEdit:9770339] Stephan, Ralf, 2022-04-04 |
| text | In a SARS-CoV-2 infection the cellular protease furin cleaves the spike protein at the S1/S2 site and that cleavage is essential for S-protein-mediated cell-cell fusion and entry into human lung cells. The furin cleavage site promotes increased spike cleavage that has implications for pathogenesis (Hoffman et al. 2020; Johnson et al, 2021). Furin is associated with the plasma membrane of host cells and mediates the hydrolytic cleavage of SARS-CoV-2 Spike (S) protein associated with ACE2. Spike cleavage by furin is affected by O-glycosylations around the cleavage site at position 685-686. In particular the P681 mutation, which occurs in the SARS-CoV-2 alpha and delta variants, results in decreased O-glycosylation, increased furin cleavage, and increased syncytia formation which may contribute to increased viral infectivity (Zhang et al, 2021a). Heparin binding to SARS-CoV-2 spike (S) effectively inhibits its cleavage into S1, S2 by furin. Unfractionated heparin (UFH) exhibits a higher furin inhibitory potency than the low-molecular-weight heparin (LMWH) (Paiardi et al, 2021). However, cleavage at the S1/S2 site occurs to some extent even if furin is absent, presumably due to the action of other proprotein convertases (Papa et al, 2021; Jaimes et al, 2020; reviewed by Takeda, 2022). Additionally it appears that, in the absence of furin-mediated priming of S, TMPRSS2 promotes the secretion of a shed form of ACE2 (sACE2) that favors cell-to-cell fusion (Essalmani et al, 2022). |
| (summation) | [Reaction:9769949] FURIN Mediated SARS-CoV-2 Spike Protein Cleavage [Homo sapiens] |
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