@article{mbs:/content/journal/jgv/10.1099/0022-1317-65-4-761, author = "Walsh, Edward E. and Schlesinger, Jacob J. and Brandriss, Michael W.", title = "Purification and Characterization of GP90, One of the Envelope Glycoproteins of Respiratory Syncytial Virus", journal= "Journal of General Virology", year = "1984", volume = "65", number = "4", pages = "761-767", doi = "https://doi.org/10.1099/0022-1317-65-4-761", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-65-4-761", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "RSV", keywords = "glycoprotein", keywords = "purification", abstract = "SUMMARY The large glycoprotein, GP90, of respiratory syncytial virus (RSV) was purified by affinity chromatography using a monoclonal antibody. Hyperimmune rabbit antiserum directed specifically to the purified GP90 neutralized RSV to high titre but did not inhibit fusion of previously infected cells. 125I-labelled GP90 bound rapidly to HEp-2 cells in an unsaturable manner; binding was inhibited by the hyperimmune rabbit antiserum.", }