| + |
S | form complex 
binding
|
Spike protein-ACE2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260287 |
|
|
Chlorocebus aethiops |
Vero Cell |
| pmid |
sentence |
| 18554741 |
Cell entry of severe acute respiratory syndrome coronavirus (SARS-CoV) is mediated by the viral spike (S) protein. Amino acids 319-510 on the S protein have been mapped as the receptor-binding domain (RBD), which mediates binding to the SARS-CoV receptor angiotensin converting enzyme 2 (ACE2) on SARS-CoV susceptible cells. Here, we demonstrate that the RBD spike protein alone can be internalized together with ACE2. We propose that after binding to ACE2, the RBD spike protein activates the ACE2 mediated cellular endocytosis signal pathway, by which SARS-CoV enters the susceptible cells. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | SARS-CoV ATTACHMENT AND ENTRY |
| + |
ACE2 | form complex
binding
|
Spike protein-ACE2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260288 |
|
|
Chlorocebus aethiops |
Vero Cell |
| pmid |
sentence |
| 18554741 |
Cell entry of severe acute respiratory syndrome coronavirus (SARS-CoV) is mediated by the viral spike (S) protein. Amino acids 319-510 on the S protein have been mapped as the receptor-binding domain (RBD), which mediates binding to the SARS-CoV receptor angiotensin converting enzyme 2 (ACE2) on SARS-CoV susceptible cells. Here, we demonstrate that the RBD spike protein alone can be internalized together with ACE2. We propose that after binding to ACE2, the RBD spike protein activates the ACE2 mediated cellular endocytosis signal pathway, by which SARS-CoV enters the susceptible cells. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | SARS-CoV ATTACHMENT AND ENTRY |
| + |
Spike protein-ACE2 | up-regulates 
|
AP-2/clathrin vescicle |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260711 |
|
|
|
|
| pmid |
sentence |
| 17522231 |
These results suggest that when SARS-CoV binds ACE2 it is internalized and penetrates early endosomes in a clathrin-dependent manner |The clathrin-dependent endocytosis is initiated by the binding of adaptor protein 2 (AP2) complexes to the cytoplasmic tail of the cell-surface receptors, which recruits clathrins |
|
| Publications: |
1 |
| Pathways: | SARS-CoV ATTACHMENT AND ENTRY |
| + |
Spike protein-ACE2 | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260289 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554741 |
Endocytosis of the Receptor-Binding Domain of SARS-CoV Spike Protein Together With Virus Receptor ACE2. Here, we demonstrate that the RBD spike protein alone can be internalized together with ACE2. We propose that after binding to ACE2, the RBD spike protein activates the ACE2 mediated cellular endocytosis signal pathway, by which SARS-CoV enters the susceptible cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SARS-CoV ATTACHMENT AND ENTRY |
3.0
Spike protein-ACE2
CPX-5683