Abstract
The expression of chimeric proteins was performed for the localization of monoclonal antibody (MAb) epitopes and functional domains in the hemagglutinin (H) protein of measles virus. The fusion helper function of the H protein was ablated by a single amino acid substitution at residue 98. Loss of reactivity to MAb 79-XV-V17 and to MAbs 16-CD-11 and 80-II-B2 was attributed to substitutions between residues 211 and 291 and between 451 and 505, respectively. The 80-II-B2 MAb epitope also seemed to be within a domain required for hemadsorption and hemagglutination activities.
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