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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.

Original publication

DOI

10.1099/0022-1317-73-9-2217

Type

Journal article

Journal

J Gen Virol

Publication Date

09/1992

Volume

73 ( Pt 9)

Pages

2217 - 2223

Keywords

Animals, Antibodies, Monoclonal, Antigens, Viral, Binding, Competitive, Cattle, Epitopes, HN Protein, Mice, Mice, Inbred BALB C, Mutagenesis, Respiratory Syncytial Viruses, Respirovirus Infections, Viral Envelope Proteins, Viral Fusion Proteins, Viral Proteins