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1 Servicio de Biologia Molecular, Centro Nacional de Microbiologia, Instituto de Salud "Carlos III", Majadahonda, 28220 Madrid, Spain
2 AFRC Institute for Animal Health, Compton, Nr Newbury, Berkshire RG16 0NN, U.K.
3 Department of Microbiology, University of Alabama Medical School, Birmingham, Alabama 35294, U.S.A.
and4 Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, C.P. 100, Laval, Québec, Canada H7N 4Z3
Two antigenic sites recognized by neutralizing monoclonal antibodies (MAbs) directed against the fusion (F) glycoprotein of human respiratory syncytial virus were mapped on the primary structure of the protein by (i) the identification of amino acid substitutions selected in antibody-escape mutants and (ii) the reactivity of synthetic peptides with MAbs. The first site contained several overlapping epitopes which were located within the trypsin-resistant amino-terminal third of the large F1 subunit. Only one of these epitopes was faithfully reproduced by a short synthetic peptide; the others might require specific local conformations to react with MAbs. The second antigenic site was located in a trypsin-sensitive domain of the F1 subunit towards the carboxy-terminal end of the cysteine-rich region. One of these epitopes was reproduced by synthetic peptides. In addition, mutagenized F protein with a substitution of serine for arginine at position 429 did not bind MAbs to the second site. These results are discussed in terms of F protein structure and the mechanisms of virus neutralization.
Received 20 March 1992;
accepted 11 May 1992.
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