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Spike Protein RBD
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P0DTC2 |
|---|---|
| Species | SARS-CoV-2 |
| Sequence | Arg319-Ser591 |
| Biological Activity | This protein is validated to bind with human ACE2 (Cat. No. Z03516) in functional ELISA assay. |
| Expression System | Human Cells |
| Formulation | Supplied as a solution in PBS, pH 7.4, 0.1% ProClin 300. |
| Storage & Stability | Upon receiving, this product remains stable for up to 3 months at 2-8°C. Protect from light. |
| Gene ID | 43740568 |
|---|---|
| Other Names | Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099}, S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099}, E2 {ECO:0000255|HAMAP-Rule:MF_04099}, Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099}, Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099}, Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099}, Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099}, S {ECO:0000255|HAMAP-Rule:MF_04099} |
| Target Background | Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the virus that causes coronavirus disease 2019 (COVID-19), the respiratory illness responsible for the COVID-19 pandemic. SARS-CoV-2 also known as 2019-nCoV, is a positive-sense single-stranded RNA virus and is believed to have zoonotic origins and has close genetic similarity to bat coronaviruses. The receptor binding domain (RBD) of spike protein of the SARS-CoV-2 virus binds Angiotensin-Converting Enzyme 2 (ACE2) to invade the host cells. Based on structural biology studies, the RBD can be oriented either in the up/standing or down/lying state with the up/standing state associated with higher pathogenicity. |
| Name | S {ECO:0000255|HAMAP-Rule:MF_04099} |
|---|---|
| Function | [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed:34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis leading to fusion of the virion membrane with the host endosomal membrane (PubMed:32075877, PubMed:32221306). Alternatively, may use NRP1/NRP2 (PubMed:33082294, PubMed:33082293) and integrin as entry receptors (PubMed:35150743). The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels (PubMed:33082293). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270). |
| Cellular Location | Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32979942}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:34504087}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:34504087}; Single- pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:34504087}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion (PubMed:34504087). An average of 26 +/-15 S trimers are found randomly distributed at the surface of the virion (PubMed:32979942) {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32979942, ECO:0000269|PubMed:34504087} |
Research Areas
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Cat# PVGS1575
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