The fusion glycoprotein of Sendai virus: sequence analysis of an epitope involved in fusion and virus neutralization.

To localize the amino acid residues on the F glycoprotein that are involved in Sendai virus fusion and virus neutralization, an anti-F monoclonal antibody which inhibits these functions was used to select three antigenic variants. Sequence analysis of the entire F gene of the three variants identified a single mutation that was responsible for the loss of antibody binding. The mutation, a proline to glutamine substitution at residue 399, was at a position in the primary sequence far removed from the hydrophobic F1-NH2 terminus thought to be directly involved in fusion. A synthetic peptide, comprising amino acid sequences in the region of the mutation, bound to the antibody used to select the variants, suggesting that the site of mutation is also the site of antibody binding. This information suggests that in the three-dimensional structure of the F molecule the amino acid residues around proline 399 are located close to the F1-NH2 terminus, and that fusion is directly inhibited by antibody binding. Other less likely alternatives are discussed.