Pre-Glycoprotein Polyprotein Gp Complex (GPC) (TCRVsSgp1) Tacaribe Virus Recombinant Protein

Function: Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion

By similarity.Glycoprotein G1 mediates virus attachment to host receptor. This interaction leads to virion entry into the host cell through the endosomal pathway

By similarity.Glycoprotein G2 is a 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 irreversable conformational changes induced upon acidification in the endosome

By similarity.

Subunit structure: Glycoprotein G1 is a homotrimer; disulfide-linked. Glycoprotein G2 is a homotrimer. GP2 homotrimers bind with GP1 homotrimers to form, with the stable signal peptide, the GP-complex. GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions supposely induce virion budding

By similarity.

Subcellular location: Stable signal peptide: Virion membrane; Multi-pass membrane protein

Potential. Host cell membrane; Multi-pass membrane protein

Potential. Glycoprotein G1: Virion membrane; Peripheral membrane protein

Potential. Host cell membrane; Peripheral membrane protein

Potential. Glycoprotein G2: Virion membrane; Single-pass membrane protein

Potential. Host cell membrane; Single-pass membrane protein

Potential. Note: Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly

By similarity.

Domain: The cytoplasmic domain of GP2 binds to the SSP

By similarity.

Post-translational modification: Cleavage by signal peptidase releases the stable signal peptide, which stays associated to the glycoprotein complex through interaction with glycoprotein G2

By similarity.Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions

By similarity.

Sequence similarities: Belongs to the arenaviridae GPC protein family.