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The Targeron Therapeutics Platform
Meeting the world’s big unmet needs in the fields of oncology and viral infection
Despite the recent clinical success in cancer immunotherapeutics and immune checkpoint inhibitors, there is a great need to develop novel strategies to enhance host immunity in cancer. Similarly, due to constant emergence of diverse viral diseases, the need for readily available broad-spectrum antivirals has never been greater.
Targeron Therapeutics has developed proprietary technology that employs first-in-class Phosphatidylserine-targeting fusion proteins that hone into and target diseased tissues. Our approach combines fusion of a phosphatidylserine binding GLA domain to a type I/type III Interferon (IFN) fusion protein (IFN-β-IFN-λ) that combines the action of two types of IFNs. Together, these biologics possess strong immunostimulatory functions into a single polypeptide molecule. Our lead biologics show promising activity in both cancer and infection models by stimulating a natural and potent host innate immune responses to fight disease.
Scientific innovation and concept development
The initial antiviral response was assumed to be exclusively mediated by type I IFNs (IFN-α/β). However, in 2003 a novel group of IFNs, type III IFNs (IFN-λs), which activate antiviral protection independently of IFN-α/β (Rutgers-awarded US patents 8,715,637 and 7,820,793) was discovered. Although, type I and type III IFNs have very similar biological activities, they signal through different receptors which have distinct pattern of tissue distribution in vivo, therefore limiting activities of type I and type III IFNs to specific cellular subsets.
Since many viruses infect multiple cell types and mice deficient in both IFN-α/β and IFN-λ signaling are more susceptible to viral infections, than single IFN receptor-deficient animals, we reasoned that a combination of IFN-α/β and IFN-λ should provide the most effective protection against both systemic and mucosal viral infections. Similarly, tumor cells of epithelial origin are more sensitive to IFN-λs, whereas endothelial and immune cells are only responsive to IFN-α/β. Therefore, we have developed novel IFN-β-IFN-λ fusion protein joining both IFN types in a single polypeptide (US patent 11,292,823) allowing simplified production and synergistic activities due to the higher receptor affinity of the fusion polypeptide. To reduce undesirable off-target effects of IFNs, we added phosphatidylserine (PS)-binding Gla domain of Gas6 protein that should preferentially localize IFNs to the sites of infection or tumor growth ((US patent 11,352,404). Moreover, Gas6-IFN-β-IFN-λ also contains 4 EGF-like domains of Gas6 that facilitate enhanced IFN signaling in the presence of PS further augmenting the antiviral and anti-tumor IFN activities of the fusion polypeptide.