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. 1990 Aug;64(8):3804–3809. doi: 10.1128/jvi.64.8.3804-3809.1990

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 1, M Gore 1, D Marchadier 1, H S Niu 1, H M Bunschoten 1, L Otvos Jr 1, W H Wunner 1, H C Ertl 1, A D Osterhaus 1, H Koprowski 1
PMCID: PMC249675  PMID: 1695255

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.

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Selected References

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