@article{mbs:/content/journal/jgv/10.1099/vir.0.81481-0, author = "Branigan, Patrick J. and Day, Nicole D. and Liu, Changbao and Gutshall, Lester L. and Melero, José A. and Sarisky, Robert T. and Vecchio, Alfred M. Del", title = "The cytoplasmic domain of the F protein of Human respiratory syncytial virus is not required for cell fusion", journal= "Journal of General Virology", year = "2006", volume = "87", number = "2", pages = "395-398", doi = "https://doi.org/10.1099/vir.0.81481-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.81481-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", 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.", }