Enterovirus D68 VP1 Protein (sf9, Fc)

Enterovirus D68, a member of Enterovirus genus of the Picornaviridae family, mainly causes respiratory system-related diseases as well as neurological complications in some patients. The capsid of Enterovirus D68 virus is composed of subunit proteins (VP1, VP2, VP3, and VP4). VP1 protein contains multiple epitopes and receptor binding sites and is often used in phylogenetic analysis of viruses. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. In addition, after binding to the host receptor, the capsid undergoes conformational changes. Enterovirus D68 VP1 Protein (sf9, Fc) is the recombinant Virus-derived Enterovirus D68 VP1 protein, expressed by Sf9 insect cells , with C-hFc labeled tag.

Enterovirus D68 (EV-D68), a member of Enterovirus genus of the Picornaviridae family, mainly causes respiratory system-related diseases as well as neurological complications in some patients. The capsid of EV-D68 virus is composed of subunit proteins (VP1, VP2, VP3, and VP4). VP1, VP2 and VP3 are located on the surface of the viral capsid; the VP4 protein is relatively small, and the viral RNA is located inside the capsid. VP1 protein contains multiple epitopes and receptor binding sites and is often used in phylogenetic analysis of viruses. VP1 is the most fully exposed of the four capsid proteins and plays a role in binding to receptors. The BC-loop of the VP1 protein contains serotype-specific antigenneutralizing sites, which can be used to distinguish virus serotypes. The folded internal hydrophobic pocket of VP1 “jelly rolls” into a lipid molecule, the “pocket factor”, which plays a role in stabilizing the structure of the virus. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. In addition, after binding to the host receptor, the capsid undergoes conformational changes^[1].

Virus

Sf9 insect cells

C-hFc

AAR98503.1 (S553-T861)

37616478  [NCBI]

Approximately 60.8 kDa

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

<1 EU/μg, determined by LAL method.