Generation of polyclonal antibodies directed against G protein-coupled receptors using electroporation-aided DNA immunization

Generation and characterization of rendomab-B1, a monoclonal antibody displaying potent and specific antagonism of the human endothelin B receptor

“…[24][25][26] To this end, we produced a panel of 27 murine mAbs targeting human ETBR using an original electroporation-aided DNA immunization strategy that favors the production of pharmacologically active antibodies directed against the native form of membrane-spanning proteins. [27][28][29] Competition binding tests, performed early during the screening process, revealed that, among these specific anti-hETBR antibodies, only one displayed very strong antagonist properties and thus appeared particularly suited to our purpose. This antibody was named rendomab-B1 and was selected for further detailed in vitro characterization, which is described here.…”

“…24 To bypass this major problem, which arises from the difficulty of producing large quantities of stable and correctly folded GPCRs, we used an electroporation-aided DNA immunization approach involving in vivo immunogen production and folding. As previously described by different groups 27,28,35,36 including ours, 29,37 this technique has been successfully used to generate polyclonal and monoclonal antibodies against the native conformation of GPCRs. The advantage of this technique is once more illustrated in the present study, since we obtained 27 mAbs recognizing native hETBR.…”

Therapeutic antibodies directed at G protein-coupled receptors

“…A similar approach was successful after injection of plasmid DNA into Lewis rats generating polyclonal antibodies against the viral GPCRs pBILF1 and pR78. 92 Again, no functional activity of these antibodies has been described so far.…”

Constitutively Active Viral Chemokine Receptors: Tools for Immune Subversion and Pathogenesis

“…BILF1 expression is restricted to the lytic phase of infection and is not associated to any of the latency programs [14,91,92]. This vGPCR is hypothesized to belong the class of chemokine receptors, presenting a low homology to CXCR4 [70], but so far no chemokines have been found to bind to this receptor.…”