Structural highlights
FunctionV9VG48_LASV Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha-DG) at the cell surface. This attachment induces virion internalization apparently through macropinocytosis. Following endocytosis, there is a pH-dependent switch from binding DAG1 to the host lysosomal receptor LAMP1. This latter binding triggers the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur. Down-modulates host DAG1.[HAMAP-Rule:MF_04084] Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification.[HAMAP-Rule:MF_04084] Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.[HAMAP-Rule:MF_04084] Contents | ||||||||||||||||||
This page was last modified 05:39, 7 June 2023.