| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.G.12.1.1 | Avian leukosis virus (RSV) envelope glycoprotein, gp95 or EnvA (606aas; 2 TMSs, N- aqnd C-terminal). Mediates pore formation preceded by a relatively stable hemifusion-like intermediate (Jha et al., 2011). A shorter version is of 138 aas and has two TMSs at the N- and C-termini. It's acc# is H7CEB0. The fusion peptide is 28 aas with a single TMS (Apellániz et al. 2014). | Viruses |
Pararnavirae, Artverviricota | EnvA of Rous sarcoma virus (Avian leukosis virus) (P03397) |
|
1.G.12.2.1 | Cat envelope syncytin-Car1 protein, a fusogenic endogenous retrovirus-derived envelope protein of 473 aas and 2 TMSs, N- and C-terminal. | Eukaryota |
Metazoa, Chordata | Syncytin-Car1 of Felis catus |
|
1.G.12.2.2 | Ebola virus glycoportein 2, GP2, of 676 aas and 2 TMSs, N- and C-terminal. The NMR structure of the internal fusion loop of 54 aas has been solved (2LCY) The fusion peptide is 17 aas long (Apellániz et al. 2014). The GP2 protein also encodes the GP2-δ peptide of 40 aas which is a viroporin (He et al. 2017). This nonstructural polypeptide, called the delta peptide, is produced in abundance during Ebola virus infection. Full length and conserved C-terminal delta peptide fragments permeabilize the plasma membranes of nucleated cells, increase ion permeability across confluent cell monolayers and permeabilize synthetic lipid bilayers. Permeabilization activity is dependent on the disulfide bond between the two conserved cysteines. The conserved C-terminal portion of the peptide is biochemically stable in human serum, and most serum-stable fragments have full activity (He et al. 2017). | Viruses |
Orthornavirae, Negarnaviricota | GP2 of Zaire Ebola virus |
|
1.G.12.2.3 | Glycoprotein 2, GP2, of 320 aas and 2 TMSs, one N-terminal and one C-terminal. A 3-stage mechanism of action has been discussed and reviewed (Apellániz et al. 2014) (see family description). | Viruses |
Mononegavirales | GP2 of Llovia virus |
|
1.G.12.2.4 | Full virion envolope spike glycoprotein, GP1.2, of 681 aas and 2 TMSs, N- and C-terminal. The intervan fusion peptide is 15 aas long (Apellániz et al. 2014). | Viruses |
Orthornavirae, Negarnaviricota | GP1.2 of Ravn Virus |
|
1.G.12.2.5 | The small secreted glycoprotein GP2 of 364 aas, containing the viroporin, GP2-δ, the last 40 aas of GP2 of Zaire ebolavirus (He et al. 2017). This nonstructural polypeptide, called the delta peptide, is produced in abundance during Ebola virus infection. Full length and conserved C-terminal delta peptide fragments permeabilize the plasma membranes of nucleated cells, increase ion permeability across confluent cell monolayers and permeabilize synthetic lipid bilayers. Permeabilization activity is dependent on the disulfide bond between the two conserved cysteines. The conserved C-terminal portion of the peptide is biochemically stable in human serum, and most serum-stable fragments have full activity (He et al. 2017). This glycoprotein interacts with cholesterol to enhance membrane fusion and cell entry (Lee et al. 2021). | Viruses |
Orthornavirae, Negarnaviricota | GP2 of Ebola virus (EBOV) |