IMPROVED PROPERTIES OF HUMAN INTERFERON-ALPHA CONFERRED BY O-GLYCOSYLATION IN MAMMALIAN CELLS

CEAGLIO, NATALIA; TARDIVO, MARÍA BELÉN; GUGLIOTTA, AGUSTINA; CRAVERO, DIANELA; ETCHEVERRIGARAY, MARINA; KRATJE, RICARDO; OGGERO, MARCOS

Barcelona

Congreso; 24th Meeting of the European Society for Animal Cell Technology (ESACT); 2015

European Society for Animal Cell Technology (ESACT)

Human interferon (hIFN)-a family consists of small proteins that exert antiviral, antiproliferative and immunomodulatory activities. Recombinant hIFN-a2b (rhIFN-a2b) is the current treatment for chronic hepatitis and some types of cancers; however, therapy outcomes have not been completely satisfactory. The short serum half-life and rapid clearance of the cytokine account for its low in vivo biological activity. For this reason, frequent administration of IFN is needed in order to achieve the desired therapeutic action, leading to patient inconvenience by producing the well-known IFN-a side effects. Therefore, applying strategies to improve the pharmacokinetic properties of this protein is relevant, aiming to increase its in vivo biological activity and, consequently, its clinical efficacy.