The Generation of Dual-Targeting Fusion Protein PD-L1/CD47 for the Inhibition of Triple-Negative Breast Cancer.
Yanlin BianTong LinTanja JakosXiaodong XiaoJianwei ZhuPublished in: Biomedicines (2022)
Triple-negative breast cancer (TNBC) is a highly aggressive subset of breast cancer with limited therapeutic options. However, its immune evasion mechanisms, characterized by the over-expression of the immune checkpoint molecules PD-L1 and CD47, can be targeted in order to facilitate cancer elimination by cells of innate and adaptive immunity. In this paper, we describe the design, preparation, and evaluation of three novel dual-targeting fusion proteins that were based on the structure frame of prototype IAB (innate and adaptive dependent bispecific fusion protein) and the "Orcutt-type IgG-scFv" molecular model. Three molecules with different spatial conformations were designed to improve antigen-antibody affinity by the addition of Ag-Ab binding sites from the variable region sequences of the anti-PD-L1 monoclonal antibody (mAb) atezolizumab and CV1, a high-affinity receptor of CD47. The results showed that the best-performing among the three proteins designed in this study was protein Pro3; its CV1 N-terminus and Fc domain C-terminus were not sterically hindered. Pro3 was better at boosting T cell proliferation and the engulfment of macrophages than the IAB prototype and, at the same time, retained a level of ADCC activity similar to that of IAB. Through improved design, the novel constructed dual-targeting immunomodulatory protein Pro3 was superior at activating the anti-tumor immune response and has thus shown potential for use in clinical applications.
Keyphrases
- immune response
- monoclonal antibody
- cancer therapy
- cell proliferation
- anti inflammatory
- binding protein
- induced apoptosis
- poor prognosis
- dendritic cells
- signaling pathway
- protein protein
- toll like receptor
- papillary thyroid
- wastewater treatment
- pi k akt
- single molecule
- young adults
- cell death
- squamous cell carcinoma
- molecularly imprinted
- highly efficient
- tandem mass spectrometry