Localization of a neutralizing epitope on the envelope protein of dengue virus type 2.
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.
Lin
B
B
Department of Microbiology, Monash University, Clayton, Victoria, Australia.
Parrish
C R
CR
Murray
J M
JM
Wright
P J
PJ
D000911:Antibodies, Monoclonal / Q000276:immunology*; D000914:Antibodies, Viral / Q000276:immunology; D001483:Base Sequence; D017931:DNA Primers / Q000737:chemistry; D003716:Dengue Virus / Q000276:immunology*; D000939:Epitopes; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009500:Neutralization Tests; D011489:Protein Denaturation; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D017931:DNA Primers; C051821:E-glycoprotein, Dengue virus type 2; D000939:Epitopes; D014759:Viral Envelope Proteins