Form
Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 10% glycerol, 5 % trehalose and 5 % mannitol.
Molecular Mass
Recombinant Human RSV-F comprises 518 amino acids with a predicted molecular mass of 58 kDa. The RSV F0 precursor protein is cleaved into the disulfide-linked F1 and F2 subunits. As a result of glycosylation, the apparent molecular mass of the protein is approximately 45-55 kDa and 18 kDa in SDS-PAGE under reducing conditions, corresponding to the two subunits respectively.
Background
During virus entry, induces fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. The fusogenic activity is inactive untill entry into host cell endosome, where a furin-like protease cleaves off a small peptide between F1 and F2 (PubMed:18216092). Interacts directly with heparan sulfate and may participates in virus attachment (PubMed:10864656). Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity (PubMed:11493675). Later in infection, proteins F expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis (PubMed:12663767).