ADU-1805 is a humanized monoclonal IgG2 antibody, a selective, pan-allelic anti- SIRPα antibody, with a K d value of 11.0 × 10 -9 M for hSIRPαV1. ADU-1805 binds to all known hSIRPα alleles. ADU-1805 blocks the SIRPα - CD47 interaction, promotes phagocytosis of cells, and enhances trogocytosis of cells. ADU-1805 can be used in research related to Burkitt lymphoma [1].
In Vivo, ADU-1805 (0.3-30 mg/kg; i.v.; single 15-minute infusion) is well tolerated in healthy cynomolgus monkeys, with stable hemoglobin levels and no observed toxicity over 59 days[1].
In Vitro, ADU-1805 binds to hSIRPαV1 with a Kd value of 11.0 × 10-9 M, and exhibits binding properties similar to those of the parental and chimeric hSIRPα.40A antibody variants[1]. ADU-1805 potently binds to primary monocytes and neutrophils, while exhibits extremely weak binding to lymphocytes[1]. ADU-1805 (0.67-66.7 nM; 2 h) promotes Rituximab -mediated phagocytosis of Raji Burkitt's lymphoma cells by peripheral blood-derived macrophages in a concentration-dependent manner[1]. ADU-1805 (0.067-66.7 nM; 2 h) enhances Rituximab-mediated trogocytosis of primary neutrophils against BJAB Burkitt's lymphoma cells in a concentration-dependent manner[1]. ADU-1805 does not bind to primary red blood cells or platelets, nor does it induce hemagglutination of red blood cells[1]. ADU-1805 (5 days) neither inhibits T cell activation nor reduces T cell counts in allogeneic mixed lymphocyte reactions[1]. ADU-1805 (100 μg/mL; 3 days) does not inhibit SEB-induced T cell activation and proliferation[1].
References:
[1]. Voets E, et al. Functional characterization of the selective pan-allele anti-SIRPα antibody ADU-1805 that blocks the SIRPα-CD47 innate immune checkpoint. J Immunother Cancer. 2019;7(1):340. Published 2019 Dec 4.
In Vivo, ADU-1805 (0.3-30 mg/kg; i.v.; single 15-minute infusion) is well tolerated in healthy cynomolgus monkeys, with stable hemoglobin levels and no observed toxicity over 59 days[1].
In Vitro, ADU-1805 binds to hSIRPαV1 with a Kd value of 11.0 × 10-9 M, and exhibits binding properties similar to those of the parental and chimeric hSIRPα.40A antibody variants[1]. ADU-1805 potently binds to primary monocytes and neutrophils, while exhibits extremely weak binding to lymphocytes[1]. ADU-1805 (0.67-66.7 nM; 2 h) promotes Rituximab -mediated phagocytosis of Raji Burkitt's lymphoma cells by peripheral blood-derived macrophages in a concentration-dependent manner[1]. ADU-1805 (0.067-66.7 nM; 2 h) enhances Rituximab-mediated trogocytosis of primary neutrophils against BJAB Burkitt's lymphoma cells in a concentration-dependent manner[1]. ADU-1805 does not bind to primary red blood cells or platelets, nor does it induce hemagglutination of red blood cells[1]. ADU-1805 (5 days) neither inhibits T cell activation nor reduces T cell counts in allogeneic mixed lymphocyte reactions[1]. ADU-1805 (100 μg/mL; 3 days) does not inhibit SEB-induced T cell activation and proliferation[1].
References:
[1]. Voets E, et al. Functional characterization of the selective pan-allele anti-SIRPα antibody ADU-1805 that blocks the SIRPα-CD47 innate immune checkpoint. J Immunother Cancer. 2019;7(1):340. Published 2019 Dec 4.