DP47-IL-2v

DP47-IL-2v is an experimental recombinant fusion protein consisting of a non-binding human IgG1 antibody (DP47) and an engineered interleukin-2 variant (IL-2v). The IL-2v component is specifically designed with abolished binding to the high-affinity IL-2 receptor alpha (IL-2Rα, CD25) to minimize the activation of regulatory T cells (Tregs) and reduce the risk of vascular leak syndrome. Instead, it selectively targets the intermediate-affinity IL-2 receptor beta and gamma chains (IL-2Rβγ), which are predominantly expressed on cytotoxic CD8+ T cells and natural killer (NK) cells, thereby promoting anti-tumor immune responses. The DP47 portion is a germline-encoded antibody scaffold that does not recognize any known human antigens. Consequently, DP47-IL-2v serves as an "untargeted" control in preclinical and translational research to differentiate the systemic effects of IL-2v signaling from the localized effects achieved by targeted immunocytokines, such as those directed against PD-1 or FAP. It was developed by Roche and Genentech for use in oncology research.

Other names

Untargeted IL-2vNon-binding IL-2v controlDP47-IL2 variantDP-47-IL2 variantDP 47-IL2 variant