The stable signal peptide (SSP) is cleaved and functions as a signal peptide. In addition, it is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome (Potential).
|CAT||Product Name||Target Species||Antibody Clone||Antibody Host||Epitope||HLA||Vector Type|
|TCR-C087Z||Mouse anti-GPC T cell receptor, pCDTCR1||LCMV||Mouse||KAVYNFATC||H-2Kb||Lentiviral|
|CAT||Product Name||Clone||Promotor||Packaging System||Targeting Diseases|
|VP-TCR-C171||Lenti-GPC T cell receptor Viral Particle||CMV||Lentivirus|
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