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Virology. 1994 Aug 1;202(2):885-90.

Localization of a neutralizing epitope on the envelope protein of dengue virus type 2.

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Department of Microbiology, Monash University, Clayton, Victoria, Australia.


Two neutralization-resistant variants of dengue virus type 2 were selected using the neutralizing monoclonal antibody G8D11. Virus N-GV4 was derived from the New Guinea C strain and virus P-GV3 from the PUO-218 strain. Both variants had an identical change at nucleotide 919 in the E gene, causing a substitution of glutamic acid for lysine at residue 307 in the E glycoprotein. The substitution abolished the ability of antibody G8D11 to bind to the E glycoprotein in radioimmunoprecipitation experiments. The epitope was sensitive to treatment with SDS and was dependent on the formation of a disulfide bridge. This dependency was determined by mutagenesis of Cys residues 11 and 12 in the E glycoprotein.

[Indexed for MEDLINE]

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