The cytoplasmic domain of the F protein of Human respiratory syncytial virus is not required for cell fusion

J Gen Virol. 2006 Feb;87(Pt 2):395-398. doi: 10.1099/vir.0.81481-0.

Abstract

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.

MeSH terms

  • Cell Fusion*
  • Cell Line
  • Humans
  • Respiratory Syncytial Virus, Human / genetics
  • Respiratory Syncytial Virus, Human / pathogenicity
  • Respiratory Syncytial Virus, Human / physiology*
  • Viral Fusion Proteins / chemistry
  • Viral Fusion Proteins / genetics
  • Viral Fusion Proteins / metabolism*

Substances

  • Viral Fusion Proteins