@article{mbs:/content/journal/jgv/10.1099/0022-1317-73-9-2217, author = "Taylor, G. and Stott, E. J. and Furze, J. and Ford, J. and Sopp, P.", title = "Protective epitopes on the fusion protein of respiratory syncytial virus recognized by murine and bovine monoclonal antibodies", journal= "Journal of General Virology", year = "1992", volume = "73", number = "9", pages = "2217-2223", doi = "https://doi.org/10.1099/0022-1317-73-9-2217", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-73-9-2217", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The regions of the fusion protein of respiratory syncytial virus (RSV) that react with neutralizing, fusion-inhibiting and highly protective bovine and murine monoclonal antibodies (MAbs) were mapped by two methods: (i) competitive binding assays and (ii) production and analysis of antibody-escape mutants. Competitive binding assays with 16 murine and 10 bovine MAbs identified 11 antigenic sites on the fusion (F) protein, many of which overlapped extensively, and indicated that cattle, a natural host for RSV, and mice recognize similar epitopes. Neutralizing MAbs identified four sites, two of which were also fusion-inhibiting and highly protective in mice. The pattern of reactivity of antibody-escape mutants with the MAbs confirmed the mapping of the protective epitopes deduced from competitive binding assays. A comparison of the biological properties of MAbs to the F protein indicated that protection against RSV infection correlated with fusion inhibition rather than neutralization titre or complement-dependent lysis of virus-infected cells.", }