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Details on Person SARS-CoV-2 fusion protein (S2', FP, fusion peptide) is a pro...
| Class:Id | Summation:9770214 |
|---|---|
| _displayName | SARS-CoV-2 fusion protein (S2', FP, fusion peptide) is a pro... |
| _timestamp | 2022-04-04 07:49:55 |
| created | [InstanceEdit:9770211] Stephan, Ralf, 2022-03-26 |
| modified | [InstanceEdit:9770279] Stephan, Ralf, 2022-04-01 [InstanceEdit:9770296] Stephan, Ralf, 2022-04-03 [InstanceEdit:9770302] Stephan, Ralf, 2022-04-04 [InstanceEdit:9770321] Stephan, Ralf, 2022-04-04 |
| text | SARS-CoV-2 fusion protein (S2', FP, fusion peptide) is a protein (458 aa) which is cleaved from the S2 fragment by TMPRSS2 and possibly other unknown host endopeptidases (Bestle et al, 2020; Navaratnarajah et al, 2021; reviewed by Takeda, 2022). S2' initiates membrane fusion by oligomerizing into an aggregated β-sheet conformation, especially when situated in cholesterol containing membrane regions. This conformation supports local membrane perturbations, a prerequisite for creation of point-like protrusions of membrane, leading to the formation of a fusion pore. Multiple membrane active regions of the Spike protein might be involved in membrane fusion in a concerted or synergistic fashion, see (Chakrabortya and Bhattacharjya, 2020) for review. In SARS-CoV-2, inhibition of actin polymerization blocked fusion, consistent with a putative role for cortical actomyosin-generated mechanical forces in fusion pore formation. Membrane cholesterol is required for fusion but is delivered via a raft-independent mechanism; cholesterol present in the plasma membrane greatly enhanced viral-spoke association and membrane fusion (Sanders et al, 2021). Of all proteins in viruses that infect humans, SARS-CoV-2 spike features the highest cysteine content, and it appears palmitoylation (a non-enzymatic modification) of these cysteines is essential for its ability to initiate membrane fusion (Sanders et al, 2021; Nguyen et al, 2021; Li et al, 2022). Additionally it appears that Ca2+-activated TMEM6 family transmembrane transport proteins, in particular ubiquitous anoctamin-6 (ANO6, TMEM16F), are essential for cell-cell fusion. TMEM16 phospholipid scramblases translocate phospholipids bidirectionally between the plasma membrane leaflets which can serve as a fusion signal (Braga et al, 2021; Whitlock & Chernomordik, 2021). |
| (summation) | [Reaction:9770187] S2 Cleavage by TMPRSS2 Exposes S2' Initiating Cell-Cell Fusion [Homo sapiens] |
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No pathways have been reviewed or authored by SARS-CoV-2 fusion protein (S2', FP, fusion peptide) is a pro... (9770214)
