United Kingdom (UK)
Recombinant monoclonal antibody to Dengue virus envelope protein. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the phage display antibody C9.
UniProt Accession Number of Target Protein: P17763
Alternative Name(s) of Target: envelope protein; envelope protein domain 3; EDIII
Immunogen: A chimeric library was created from clones that were able to bind DENV2 EDIII, this library was then panned against DENV2 EDIII to create this antibody.
Specificity: This antibody is specific for the EDIII protein of the dengue virus. The dengue virus causes the disease known as dengue fever.
Application Notes: To determine the specificity and DENV cross-reactivity of the IgG1 version of this antibody an ELISA was performed on EDIII, this antibody had strong binding for EDIII from DENV2 and to a lesser extent with EDIII from DENV1 and DENV3. Furthermore, immunofluorescence was performed on uninfected BHK-21 cells and cells infected with DENV2 using the IgG1 version of this antibody, it showed clear fluorescence in the cytoplasm of infected cells. Finally, a plaque reduction neutralization test was performed using the IgG1 version of this antibody, this antibody showed a 25% reduction of plaque formation. This antibody is a chimeric antibody with mouse Vκ/human Cκ and mouse VH/human CH segments (Moreland et al, 2012; pmid:22489114).
Antibody first published in:
Moreland et al. Phage Display Approaches for the Isolation of Monoclonal Antibodies Against Dengue Virus Envelope Domain III from Human and Mouse Derived Libraries. Int J Mol Sci. 2012; 13(3): 2618–2635. PMID:22489114
Note on publication:
A chimeric Fab-phage library was constructed from a panel of EDIII specific mouse hybridomas by pooling the VH and VL chain sequences from the hybridomas and cloning these into the pComb3X phagemid vector with human CH and CL encoding sequences. Biopanning against EDIII identified a unique antibody (C9) that cross-reacts with EDIII from DENV1-3 and, in the IgG format, binds and neutralizes DENV2 in cell-based assays.