@article{mbs:/content/journal/jgv/10.1099/0022-1317-81-7-1757, author = "Gigant, Benoit and Iseni, Frédéric and Gaudin, Yves and Knossow, Marcel and Blondel, Danielle", title = "Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization", journal= "Journal of General Virology", year = "2000", volume = "81", number = "7", pages = "1757-1761", doi = "https://doi.org/10.1099/0022-1317-81-7-1757", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-81-7-1757", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "Rabies virus (PV strain) phosphoprotein (P) was expressed in bacteria. This recombinant protein binds specifically to the nucleoprotein–RNA complex purified from infected cells. Chemical cross-linking and gel-filtration studies indicated that the P protein forms oligomers. Analytical centrifugation data demonstrated the co-existence of monomeric and oligomeric forms of rabies virus P protein and suggested that there is an equilibrium between these species. As P expressed in bacteria is not phosphorylated, this result indicates that P phosphorylation is not required for its oligomerization. Although an alignment of several rhabdovirus P sequences revealed that the amino-terminal domain of P has a conserved predicted propensity to form helical coiled coils, an amino-terminally truncated form of P protein, lacking the first 52 residues, was also shown to be oligomeric. Therefore, the amino-terminal domain of rabies virus P is not necessary for its oligomerization.", }