Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity

Documenti analoghi

• Recombinant Sendai Viruses Expressing Fusion Proteins with Two Furin Cleavage Sites Mimic the Syncytial and Receptor-Independent Infection Properties of Respiratory Syncytial Virus
  di: Rawling, Joanna, et al.
  Pubblicazione: (2011)
• The Soluble Form of Human Respiratory Syncytial Virus Attachment Protein Differs from the Membrane-Bound Form in Its Oligomeric State but Is Still Capable of Binding to Cell Surface Proteoglycans
  di: Escribano-Romero, Estela, et al.
  Pubblicazione: (2004)
• Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion
  di: González-Reyes, Luis, et al.
  Pubblicazione: (2001)
• A Chimeric Respiratory Syncytial Virus Fusion Protein Functionally Replaces the F and HN Glycoproteins in Recombinant Sendai Virus
  di: Zimmer, Gert, et al.
  Pubblicazione: (2005)
• Antigenic Structure of Human Respiratory Syncytial Virus Fusion Glycoprotein
  di: López, Juan A., et al.
  Pubblicazione: (1998)