Structural highlights
Function
GP_SFTS Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (PubMed:23388721). Plays a role in the packaging of ribonucleoproteins during virus assembly (By similarity).[UniProtKB:P09613][UniProtKB:P21401][1] Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (PubMed:23388721).[UniProtKB:P09613][UniProtKB:P21401][2]
References
- ↑ Hofmann H, Li X, Zhang X, Liu W, Kühl A, Kaup F, Soldan SS, González-Scarano F, Weber F, He Y, Pöhlmann S. Severe fever with thrombocytopenia virus glycoproteins are targeted by neutralizing antibodies and can use DC-SIGN as a receptor for pH-dependent entry into human and animal cell lines. J Virol. 2013 Apr;87(8):4384-94. PMID:23388721 doi:10.1128/JVI.02628-12
- ↑ Hofmann H, Li X, Zhang X, Liu W, Kühl A, Kaup F, Soldan SS, González-Scarano F, Weber F, He Y, Pöhlmann S. Severe fever with thrombocytopenia virus glycoproteins are targeted by neutralizing antibodies and can use DC-SIGN as a receptor for pH-dependent entry into human and animal cell lines. J Virol. 2013 Apr;87(8):4384-94. PMID:23388721 doi:10.1128/JVI.02628-12
