Structural polyprotein Protein, Barmah forest virus (Cell-Free, His)

The capsid protein is a key component of the virus. It has a spike composed of E1-E2 heterodimers and is surrounded by a lipid membrane. This protein binds to viral RNA, helping the virus evade the immune system and facilitating the trafficking of other viral proteins. Structural polyprotein Protein, Barmah forest virus (Cell-Free, His) is the recombinant Virus-derived Structural polyprotein protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of Structural polyprotein Protein, Barmah forest virus (Cell-Free, His) is 439 a.a., with molecular weight of 50.7 kDa.

The structural polyprotein plays a pivotal role in the formation of an icosahedral capsid with T=4 symmetry, comprising 240 copies of the capsid protein surrounded by a lipid membrane, featuring 80 spikes composed of E1-E2 heterodimeric trimers. Binding to the viral RNA genome, adjacent to a ribosome binding site, facilitates viral genome translation following release. The structural polyprotein possesses protease activity, leading to its autocatalytic cleavage from the nascent structural protein. Post-cleavage, it transiently associates with ribosomes, rapidly assembles into icosahedric core particles, and eventually associates with the spike glycoprotein E2 at the cell membrane, culminating in budding and mature virion formation. During infection, virions attach to target cells, undergo clathrin-mediated endocytosis, and fuse with the host endosomal membrane, releasing the nucleocapsid into the cytoplasm. This uncoating event, crucial for genomic RNA accessibility, may be triggered by the interaction of capsid proteins with ribosomes. The structural polyprotein also inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, potentially aiding the evasion of innate immune detection. Additionally, it provides the signal sequence for translocating the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1, ensuring pH protection during transport via the secretory pathway, with gradual release into the extracellular space upon virion release from the host cell.

Virus

E. coli Cell-free

N-10*His

P89946 (Y801-H1239)

1489701

YEHSTTMPNQVGIPFKALIERPGYAGLPLSLVVIKSELVPSLVQDYITCNYKTVVPSPYIKCCGGAECSHKNEADYKCSVFTGVYPFMWGGAYCFCDTENSQMSEVYVTRGESCEADHAIAYQVHTASLKAQVMISIGELNQTVDVFVNGDSPARIQQSKFILGPISSAWSPFDHKVIVYRDEVYNEDYAPYGSGQAGRFGDIQSRTVNSTDVYANTNLKLKRPASGNVHVPYTQTPSGFSYWKKEKGVPLNRNAPFGCIIKVNPVRAENCVYGNIPISMDIADAHFTRIDESPSVSLKACEVQSCTYSSDFGGVASISYTSNKVGKCAIHSHSNSATMKDSVQDVQESGALSLFFATSSVEPNFVVQVCNARITCHGKCEPPKDHIVPYAAKHNDAEFPSISTTAWQWLAHTTSGPLTILVVAIIVVVVVSIVVCARH

50.7 kDa

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

<1 EU/μg, determined by LAL method.