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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