Immunogenicity of a Purified Fragment of 170 Yellow Fever Envelope Protein

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Abstract
Information on the immunogenic properties of purified flavivirus proteins may be useful in the development of recombinant or synthetic peptide vaccines. Using a monoclonal antibody, an attempt was made to purify the envelope (E) protein of 17D yellow fever virus (17D YF) by affinity chromatography. The purified material could not be identified as intact E protein but it did bear antigenic determinants of E as determined by selective reactivity with anti-E monoclonal antibodies. Rabbits immunized with this material produced antibodies that neutralized 17DYF and dengue-2 viruses in comparable titers, indicating that cross-reactive antigenic determinants were preserved. Immunization ofmice resulted in protection against intracerebral challenge with 17D YF.