GPC Protein, Lassa virus (Cell-Free, His)

GPC proteins function to cleave the signal peptide and stabilize the spike complex. GPC Protein, Lassa virus (Cell-Free, His) is the recombinant Virus-derived GPC protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of GPC Protein, Lassa virus (Cell-Free, His) is 232 a.a., with molecular weight of 29.7 kDa.

GPC functions as a cleaved signal peptide integral to the GP complex (GP-C), playing a crucial role in stabilizing the spike complex in its native conformation. This protein is essential for various stages of the viral life cycle, including 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 pH-dependent glycoprotein-mediated cell fusion. As a component of the virion spikes, GPC, together with glycoprotein G2, forms trimers that are linked to the underlying matrix. It interacts with the host receptor and facilitates virus attachment to the primary receptor alpha-dystroglycan (DAG1) at the cell surface, leading to virion internalization through macropinocytosis. Subsequent to endocytosis, GPC undergoes a pH-dependent switch from binding to DAG1 to the host lysosomal receptor LAMP1, triggering the dissociation of GP1. This exposes the fusion subunit, GP2, facilitating the fusion process. Notably, GPC also down-modulates host DAG1, influencing the host-virus interaction dynamics.

Virus

E. coli Cell-free

N-10*His

P17332 (G259-R490)

/

GTFTWTLSDSEGNETPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIRRLKTEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSRYWYLNHTSTGKTSLPRCWLISNGSYLNETKFSDDIEQQADNMITEMLQKEYIDRQGKTPLGLVDLFVFSTSFYLISIFLHLVKIPTHRHIVGKPCPKPHRLNHMGICSCGLYKQPGVPVRWKR

29.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.