This study aimed to improve the pharmacokinetics and antitumor efficacy of human interleukin-15 (hIL-15) by genetically fusing it with a human serum albumin-specific protein binder (rHSA). The resulting fusion protein, rHSA-IL15, retained binding affinity for both the IL-15 receptor α and human serum albumin. In transgenic mice expressing human serum albumin, rHSA-IL15 exhibited a ~40-fold increase in terminal half-life compared to free hIL-15. Additionally, rHSA-IL15 enhanced the secretion of Granzyme B and IFN-γ by immune cells and expanded activated CD4⁺ and CD8⁺ T cell populations. In xenograft squamous cell carcinoma and allograft melanoma mouse models, rHSA-IL15 demonstrated significant antitumor activity through activation of NK and CD8⁺ T cells.
The rHSA-IL15 fusion protein significantly prolonged the half-life of hIL-15 and enhanced its antitumor activity by stimulating immune effector cells, suggesting its potential as a cancer immunotherapeutic agent.
Transgenic mice expressing human serum albumin (HSA), utilized to evaluate the pharmacokinetics and antitumor efficacy of the rHSA-IL15 fusion protein.
Cancer immunotherapy, Interleukin-15, Albumin fusion protein, Pharmacokinetics, T cell activation
Transgenic mouse model, Human serum albumin expression, Protein engineering, Fusion protein design
From model design to experimental results
Tailor-made solutions adapted to scientific questions
Comprehensive dataset package
Generated with biopharma partners and in-house
Scientific follow-up and advice along the project
Collaborative approach for problem solving and development of innovative models
Breeding facilities in US and Europe
Certified health status from professional breeders
