Large envelope Protein, HBV-C (P.pastoris, 180a.a, His)

The large envelope protein is crucial in its two conformations, "outside" (Le-HBsAg) and "inside" (Li-HBsAg). Externally, it binds the virus to cellular receptors, initiates infection, determines species specificity, and promotes viral particle internalization via caveolin-mediated endocytosis. Large envelope Protein, HBV-C (P.pastoris, 180a.a, His) is the recombinant Virus-derived Large envelope protein, expressed by P. pastoris , with N-6*His labeled tag.

The Large Envelope Protein exists in two topological conformations, namely 'external' or Le-HBsAg, and 'internal' or Li-HBsAg. In its external conformation, the protein acts as a critical agent, binding the virus to cell receptors and initiating infection. This pivotal interaction not only establishes species specificity and liver tropism but also triggers virion internalization, predominantly through caveolin-mediated endocytosis. The Large Envelope Protein further facilitates fusion between the virion membrane and the endosomal membrane. In its internal conformation, the protein plays a crucial role in virion morphogenesis, functioning akin to a matrix protein and mediating contact with the nucleocapsid. Simultaneously, the middle envelope protein plays a vital role in virion budding, inducing a nucleocapsid-independent process. This budding mechanism leads to the formation of subviral lipoprotein particles, with a diameter of 22 nm, devoid of a nucleocapsid.

Virus

P. pastoris

N-6*His

P31868 (G2-G181)

/

Partial

GGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPNKDHWPEANQVGVGTFGPGFTPPHGGLLGWSPQAQGILTTVPAAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSIFSRTGDPAPNMENTTSG

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.