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. Interacts directly with heparan sulfate and may participate in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. 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.
Background References
1. Watanabe M et al. Delayed activation of altered fusion glycoprotein in a chronic measles virus variant that causes subacute sclerosing panencephalitis. J Neurovirol. 1995 Jun;1(2):177-88.
2. Bolt G and Pedersen IR. The role of subtilisin-like proprotein convertases for cleavage of the measles virus fusion glycoprotein in different cell types. Virology. 1998 Dec 20;252(2):387-98.
Sequence Similarity
Belongs to the paramyxoviruses fusion glycoprotein family.
Western blot analysis of Fusion glycoprotein F0 on Fusion glycoprotein F0 transfected HEK293 cell lysates using anti- Fusion glycoprotein F0 antibody at 1/500 dilution.
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