Journal of General Virology · 2006 · 23 citations · 21 references
Life SciencesInfectious DiseasesMolecular BiologyMolecular VirologyStructural BiologyVirologyViral AssemblyViral InfectionsViral PathogenesisViral Protein ProcessingViral StructureVirus-host InteractionsRecombinant Fusion ProteinsViral Fusion MechanismsViral Fusion ProteinsViral Membrane FusionViral Protein TraffickingViral Surface Proteins
The cytoplasmic domains of the fusion proteins encoded by several viruses play a role in cell fusion and contain sites for palmitoylation associated with viral protein trafficking and virus assembly. The fusion (F) protein of Human respiratory syncytial virus (HRSV) has a predicted cytoplasmic domain of 26 residues containing a single palmitoylated cysteine residue that is conserved in bovine RSV F protein, but not in the F proteins of other pneumoviruses such as pneumonia virus of mice, human metapneumovirus and avian pneumovirus. The cytoplasmic domains in other paramyxovirus fusion proteins such as Newcastle disease virus F protein play a role in fusion. In this study, it was shown that deletion of the entire cytoplasmic domain or mutation of the single cysteine residue (C550S) of the HRSV F protein had no effect on protein processing, cell-surface expression or fusion.
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