title: Review of the recombinant human interferon gamma as an immunotherapeutic: Impacts of production platforms and glycosylation.
abstract: Human interferon gamma is a cytokine belonging to a diverse group of interferons which have a crucial immunological function against mycobacteria and a wide variety of viral infections. To date, it has been approved for treatment of chronic granulomatous disease and malignant osteopetrosis, and its application as an immunotherapeutic agent against cancer is an increasing prospect. Recombinant human interferon gamma, as a lucrative biopharmaceutical, has been engineered in different expression systems including prokaryotic, protozoan, fungal (yeasts), plant, insect and mammalian cells. Human interferon gamma is commonly expressed in Escherichia coli, marketed as ACTIMMUNE®, however, the resulting product of the prokaryotic expression system is unglycosylated with a short half-life in the bloodstream; the purification process is tedious and makes the product costlier. Other expression systems also did not show satisfactory results in terms of yields, the biological activity of the protein or economic viability. Thus, the review aims to synthesise available information from previous studies on the production of human interferon gamma and its glycosylation patterns in different expression systems, to provide direction to future research in this field.
authors: College of Science and Engineering, James Cook University, Townsville 4811, Queensland, Australia; Centre for Biodiscovery and Molecular Development of Therapeutics, James Cook University, Townsville 4811, Queensland, Australia.
authors: Ali
authors: A
authors: Razaghi
authors: College of Public Health, Medical and Veterinary Science, James Cook University, Townsville, Queensland, 4811, Australia.
authors: Leigh
authors: L
authors: Owens
authors: College of Science and Engineering, James Cook University, Townsville 4811, Queensland, Australia; Centre for Biodiscovery and Molecular Development of Therapeutics, James Cook University, Townsville 4811, Queensland, Australia. Electronic address: kirsten.heimann@jcu.edu.au.
authors: Kirsten
authors: K
authors: Heimann
mesh_terms: D000818:Animals; D004926:Escherichia coli; D015316:Genetic Therapy; D006031:Glycosylation; D006801:Humans; D007167:Immunotherapy; D007371:Interferon-gamma / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism / Q000627:therapeutic use; D009369:Neoplasms / Q000628:therapy; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism / Q000627:therapeutic use
chemical_list: C573415:IFNG protein, human; D011994:Recombinant Proteins; D007371:Interferon-gamma
keywords: Actimmune; Asparagine: (PubChem CID: 6267); Biopharmaceutical; Cancer immunotherapy; Fucose: (PubChem CID: 17106); Galactose: (PubChem CID: 6036); Glycosylation; Guanidinium hydrochloride: (PubChem CID: 5742); Interferon gamma; Mannose: (PubChem CID: 18950); Methionine: (PubChem CID: 6137); N-acetyl glucosamine: (PubChem CID: 24139); N-acetylneuraminic acid (PubChem CID: 439197); Oxaliplatin: (PubChem CID: 429863); Protein expression & purification; Pyroglutamate: (PubChem CID: 23668602); Sepharose: (PubChem CID: 11966311); Urea: (PubChem CID: 1176)