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J Virol. 1990 August; 64(8): 3804-3809

Structural and immunological characterization of a linear virus-neutralizing epitope of the rabies virus glycoprotein and its possible use in a synthetic vaccine.

B Dietzschold, M Gore, D Marchadier, H S Niu, H M Bunschoten, L Otvos Jr, W H Wunner, H C Ertl, A D Osterhaus and H Koprowski

Wistar Institute of Anatomy and Biology, Philadelphia, Pennsylvania 19104-4268.

ABSTRACT

We have mapped a linear epitope recognized by the virus-neutralizing monoclonal antibody 6-15C4 within the primary sequence of the G protein from the Evelyn-Rokitnicki-Abelseth strain of rabies virus. This was accomplished by using fragments of the rabies virus G protein and deduced amino acid sequences of neutralization-resistant variant rabies viruses. The monoclonal antibody 6-15C4 specifically recognized a synthetic peptide (peptide G5-24) which resembles the 6-15C4 epitope in structure. In addition, a tandem peptide constructed from the G5-24 peptide and a dominant TH cell epitope of the rabies virus N protein induced protective immunity against lethal rabies virus challenge infection in mice.


J Virol. 1990 August; 64(8): 3804-3809




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