Relation Results

Summary

Name S
Full Name Spike glycoprotein
Synonyms S glycoprotein, E2, Peplomer protein |
Primary ID P0DTC2
Links - -
Type protein
Relations 10
Pathways COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY, SARS-CoV FIBROSIS
Function attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor a ...
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Type: Score: Layout: SPV 
0.20.20.20.20.20.20.20.2TMPRSS2SFURINTMPRSS4CTSLCTSBACE2CoV2 Spike protein-ACE2CoV2 spike protein-NRP1

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Relations
Regulator
Mechanism
target
score ℹ
+ TMPRSS2up-regulates activity img/direct-activation.png cleavage S 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260736 Homo sapiens
pmid sentence
Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. The Cellular Serine Protease TMPRSS2 Primes SARS-2- S for Entry, and a Serine Protease Inhibitor Blocks SARS-CoV-2 Infection of Lung Cells
Publications: 1 Organism: Homo Sapiens
Pathways:COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY
+ FURINup-regulates activity img/direct-activation.png cleavage S 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262305 Homo sapiens Calu-3 Cell
pmid sentence
Here, we report that 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.
Identifier Residue Sequence Organism Cell Line
SIGNOR-262303 Homo sapiens Calu-3 Cell
pmid sentence
Here, we report that 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.
Publications: 2 Organism: Homo Sapiens
Pathways:SARS-CoV ATTACHMENT AND ENTRY
+ TMPRSS4up-regulates activity img/direct-activation.png cleavage S 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262304 Homo sapiens
pmid sentence
TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion.
Identifier Residue Sequence Organism Cell Line
SIGNOR-262306 Homo sapiens
pmid sentence
TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion.
Publications: 2 Organism: Homo Sapiens
Pathways:SARS-CoV ATTACHMENT AND ENTRY
+ CTSLup-regulates activity img/direct-activation.png cleavage S 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260737 Homo sapiens CACO-2 Cell
pmid sentence
SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines.
Publications: 1 Organism: Homo Sapiens
Pathways:COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY
+ CTSBup-regulates activity img/direct-activation.png cleavage S 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260738 Homo sapiens CACO-2 Cell
pmid sentence
SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines.
Publications: 1 Organism: Homo Sapiens
Pathways:COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY
+ Sdown-regulates activity img/direct_inhibition.png binding ACE2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260742 Homo sapiens
pmid sentence
SARS-CoV and likely SARS-CoV-2 lead to downregulation of the ACE2 receptor, but not ACE, through binding of the spike protein with ACE2. This leads to viral entry and replication, as well as severe lung injury.
Publications: 1 Organism: Homo Sapiens
Pathways:COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY, SARS-CoV FIBROSIS
+ Sform complex img/form-complex.png binding CoV2 Spike protein-ACE2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260739 Chlorocebus aethiops Vero Cell
pmid sentence
We report here that ACE2 could mediate SARS-CoV-2 S-mediated entry into cells, establishing it as a functional receptor for this newly emerged coronavirus. The SARS-CoV-2 SB engages human ACE2 (hACE2) with comparable affinity to SARS-CoV SB from viral isolates associated with the 2002–2003 epidemic (i.e., binding with high affinity to hACE2). Tight binding to hACE2 could partially explain the efficient transmission of SARS-CoV-2 in humans, as was the case for SARS-CoV.
Publications: 1 Organism: Chlorocebus Aethiops
Pathways:COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY
+ Sform complex img/form-complex.png binding CoV2 spike protein-NRP1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-261671 Homo sapiens HEK-293 Cell
pmid sentence
Neuropilin-1 facilitates SARS-CoV-2 cell entry and provides a possible pathway into the central nervous system To determine whether SARS-CoV-2 uses NRP1 for virus entry, we generated replication deficient lentiviruses pseudotyped with SARS-CoV-2 spike protein (S) that drive expression of green fluorescent protein (GFP) upon infection. When expressed alone, ACE2 rendered cells susceptible to infection (Fig. 1a). NRP1 alone allowed lower, yet detectable levels of infection, both in HEK-293T and in Caco2 cells (Fig. 1a,b), while cells transfected with plasmids encoding only TMPRSS2 were not infected (Fig. 1a). The co-expression of TMPRSS2 with either ACE2 or NRP1 potentiated the infection, with ACE2 together with TMPRSS2 being twice as efficient as NRP1 with TMPRSS2 (Fig. 1c)
Publications: 1 Organism: Homo Sapiens
Pathways:SARS-CoV ATTACHMENT AND ENTRY
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