PROSITE documentation PDOC51926 [for PROSITE entry PS51926]Coronavirus envelope (CoV E) protein profile
Coronaviruses (CoVs) [E1] are a diverse group of enveloped, plus-stranded RNA viruses that infect humans and many animal species, in which they can cause respiratory, enteric, hepatic, central nervous system and neurological diseases of varying severity. The main CoV structural proteins are S (spike), E (envelope), M (membrane), and N (nucleocapsid), where S, E, and M are integral membrane proteins. CoV E proteins are involved in several aspects of the virus’ life cycle, such as assembly, budding, envelope formation, and pathogenesis. They are ~100-residue-long polypeptides that are minor components in virions but are abundantly expressed inside infected cells. They are localized mainly to the endoplasmic reticulum (ER) and Golgi-complex where they participate in the assembly, budding, and intracellular trafficking of infectious virions [1,2,3,4].
Cov E proteins have a short hydrophilic N-terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C-terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [1,2,3,4].
In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape (see <PDB:2MM4>) [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other (see <PDB:5X29>) [4].
The profile we developed covers the entire CoV E protein.
Last update:June 2020 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Schoeman D. Fielding B.C. |
| Title | Coronavirus envelope protein: current knowledge. | |
| Source | Virol. J. 16:69-69(2019). | |
| PubMed ID | 31133031 | |
| DOI | 10.1186/s12985-019-1182-0 |
| 2 | Authors | Li Y. Surya W. Claudine S. Torres J. |
| Title | Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins. | |
| Source | J. Biol. Chem. 289:12535-12549(2014). | |
| PubMed ID | 24668816 | |
| DOI | 10.1074/jbc.M114.560094 |
| 3 | Authors | Teoh K.T. Siu Y.L. Chan W.L. Schluter M.A. Liu C.J. Peiris J.S. Bruzzone R. Margolis B. Nal B. |
| Title | The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis. | |
| Source | Mol. Biol. Cell. 21:3838-3852(2010). | |
| PubMed ID | 20861307 | |
| DOI | 10.1091/mbc.E10-04-0338 |
| 4 | Authors | Surya W. Li Y. Torres J. |
| Title | Structural model of the SARS coronavirus E channel in LMPG micelles. | |
| Source | Biochim. Biophys. Acta. Biomembr. 1860:1309-1317(2018). | |
| PubMed ID | 29474890 | |
| DOI | 10.1016/j.bbamem.2018.02.017 |
| E1 | Title | https://viralzone.expasy.org/30?outline=all_by_species |
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