@article{mbs:/content/journal/jgv/10.1099/0022-1317-24-3-433, author = "Sokol, Frantisek and Clark, H. F. and Wiktor, T. J. and McFalls, Marguerite L. and Bishop, D. H. L. and Obijeski, J. F.", title = "Structural Phosphoproteins associated with ten Rhabdoviruses", journal= "Journal of General Virology", year = "1974", volume = "24", number = "3", pages = "433-445", doi = "https://doi.org/10.1099/0022-1317-24-3-433", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-24-3-433", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "SUMMARY The phosphorylation of structural proteins of ten rhabdoviruses has been studied. Each virus preparation has been found to possess at least one phosphoprotein which, in the case of Chandipura, Cocal, Piry viruses or vesicular stomatitis virus (VSV), Indiana and New Jersey serotypes, is the minor NS protein. In rabies virus the sole phosphoprotein appears to be the N protein of the nucleocapsid. For Mokola and Lagos bat viruses, two or three phosphoproteins have been observed, one of which is the N protein. Spring viraemia of carp virus (SVCV) preparations contain two phosphoproteins one of which is, or has a mobility close to, that of the N protein. Kern Canyon virus preparations also possess two phosphoproteins, one with the same electrophoretic mobility as (and possible identity to), the virus glycoprotein while the other has a mobility slightly slower than the N protein. Antigenically the core proteins of rabies, Mokola and Lagos bat viruses have been shown to be related to each other but distinct from those of SVCV or VSV.", }