Fusion glycoprotein F0/F Protein, HRSV (P11209, sf9, His)

The fusion glycoprotein F0/F protein is cleaved to generate mature F1 and F2 fusion glycoproteins.It functions as a viral fusion protein, promoting the fusion of virus and cell membranes through different state transitions.Fusion glycoprotein F0/F Protein, HRSV (P11209, sf9, His) is the recombinant Virus-derived Fusion glycoprotein F0/F protein, expressed by Sf9 insect cells , with C-His labeled tag.

The Fusion glycoprotein F0/F protein is an inactive precursor undergoing cleavage at two sites by a furin-like protease to generate the mature F1 and F2 fusion glycoproteins. Functioning as a class I viral fusion protein, it operates through at least three conformational states: the pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the coiled coil regions adopt a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. This structural transition drives the apposition and subsequent fusion of viral and cellular membranes, facilitating the delivery of the nucleocapsid into the cytoplasm. Remarkably, this fusion process is pH-independent and occurs at either the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also plays a pivotal role in host cell attachment by binding to host heparan sulfate. Moreover, the F protein is instrumental in host cell entry through interaction with host IGFR1, activating PRKCZ/PKCzeta, which recruits host NCL/nucleolin to the apical cell surface, allowing binding to fusion glycoprotein F1. In later stages of infection, F protein expressed at the plasma membrane can mediate fusion with adjacent cells, leading to syncytia formation—a cytopathic effect that may result in tissue necrosis. Additionally, F protein may trigger p53-dependent apoptosis, further highlighting its diverse roles in the viral life cycle and pathogenesis.

Virus

Sf9 insect cells

C-His

P11209 (F22-T529)

/

Approximately 63 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.