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TCIDNameDomainKingdom/PhylumProtein(s)
1.G.17.1.1









Envolope glycoprotein of 341 aas and 3 TMSs, one N-terminal and two C-terminal, gPr72. Three YXXL sequences of a Bovine Leukemia Virus TEnv transmembrane protein are independently required for fusion activity by controlling expression on the cell membrane (Matsuura et al. 2019). The fusion peptide mediates fusion of the viral envelop with the cell membrane (Meher and Chakraborty 2020).

Viruses
Retroviridae
Env protein of bovine leukemia virus
1.G.17.1.2









Envelope glycoprotein of 259 aas, Env

Viruses
Retroviridae
Env of Human T-cell leukemia virus 2 (HTLV-2)
1.G.17.1.3









Envelope glycoprotein of 214 aas (partial) Gp30.

Viruses
Retroviridae
Gp30 of bovine leukemia viru
1.G.17.1.4









The Human T-cell leukemia virus 1, HTLV-1, of 488 aas and 2 TMSs, N- and C-terminal. The glycine-rich region of this transmembrane protein is involved in membrane fusion. It is a class I viral fusion protein (Wilson et al. 2005). The N-terminal fusion peptide initiates virus-cell membrane fusion. The fusion peptide is linked to the coiled-coil core through a conserved sequence that is rich in glycines. Wilson et al. 2005 investigated the functional role of the glycine-rich segment, Met-326 to Ser-337, of gp21. Alanine substitution for the hydrophobic residue Ile-334 caused a 90% reduction in cell-cell fusion activity without a detectable effect on the lipid-mixing and pore forming phases of fusion. Retroviral glycoprotein fusion thus appears to require flexibility within the glycine-rich segment and hydrophobic contacts mediated by this segment (Wilson et al. 2005).

 

Viruses
Ortervirales
HTLV-1 of T-cell leukemia virus 1