SARS-CoV-2 virions attached to the host cell surface via a c...
| created | [InstanceEdit:9699008] Gillespie, Marc E, 2020-09-05 |
| dbId | 9698991 |
| displayName | SARS-CoV-2 virions attached to the host cell surface via a c... |
| literatureReference |
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| modified | [InstanceEdit:9774254] Stephan, Ralf, 2022-05-20 |
| schemaClass | Summation |
| text | SARS-CoV-2 virions attached to the host cell surface via a complex involving viral spike (S) protein and host angiotensin-converting enzyme 2 (ACE2) can directly fuse their membrane with the host cell membrane, releasing the uncoated virion nucleocapsid into the cytoplasm. The process starts with the spike protein undergoing cleavage by furin into S1/S2, followed by cleavage of S2 catalyzed by TMPRSS2, freeing the fusion peptide (FP) which mediates membrane fusion. 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). |
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