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J. Virol., 10 1997, 7240-7245, Vol 71, No. 10
Copyright © 1997, American Society for Microbiology

Identification of an immunodominant neutralizing and protective epitope from measles virus fusion protein by using human sera from acute infection

SF Atabani, OE Obeid, D Chargelegue, P Aaby, H Whittle and MW Steward
Department of Clinical Sciences, London School of Hygiene and Tropical Medicine, United Kingdom.

Polyclonal sera obtained from African children with acute measles were used to screen a panel of 15-mer overlapping peptides representing the sequence of measles virus (MV) fusion (F) protein. An immunodominant antigenic region from the F protein (p32; amino acids 388 to 402) was found to represent an amino acid sequence within the highly conserved cysteine-rich domain of the F protein of paramyxoviruses. Epitope mapping of this peptide indicated that the complete 15-amino-acid sequence was necessary for high-affinity interaction with anti-MV antibodies. Immunization of two strains of mice with the p32 peptide indicated that it was immunogenic and could induce antipeptide antibodies which cross-reacted with and neutralized MV infectivity in vitro. Moreover, passive transfer of antipeptide antibodies conferred significant protection against fatal rodent-adapted MV-induced encephalitis in susceptible mice. These results indicate that this epitope represents a candidate for inclusion in a future peptide vaccine for measles.

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