Review of the recombinant human interferon gamma as an immunotherapeutic: Impacts of production platforms and glycosylation

Razaghi, Ali, Owens, Leigh, and Heimann, Kirsten (2016) Review of the recombinant human interferon gamma as an immunotherapeutic: Impacts of production platforms and glycosylation. Journal of Biotechnology, 240. pp. 48-60.

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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.

Item ID: 48140
Item Type: Article (Research - C1)
ISSN: 1873-4863
Keywords: protein expression & purification; glycosylation; actimmune; biopharmaceutical; cancer immunotherapy; interferon gamma
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Additional Information:

A version of this publication was included as Chapter 1 of the following PhD thesis: Razaghi, Ali (2017) Evaluation of expression systems of recombinant human interferon gamma. PhD thesis, James Cook University, which is available Open Access in ResearchOnline@JCU. Please see the Related URLs for access.

Chemical compounds studied in this article:

Asparagine: (PubChem CID: 6267)

Fucose: (PubChem CID: 17106)

Galactose: (PubChem CID: 6036)

Guanidinium hydrochloride: (PubChem CID:5742)

Mannose: (PubChem CID: 18950)

Methionine: (PubChem CID: 6137)

N-acetyl glucosamine: (PubChem CID: 24139)

N-acetylneuraminic acid (PubChem CID: 439197)

Oxaliplatin: (PubChem CID: 429863)

Pyroglutamate: (PubChem CID: 23668602)

Sepharose: (PubChem CID: 11966311)

Urea: (PubChem CID: 1176)

Funders: Advanced Manufacturing Cooperative Research Centre (AMCRC)
Projects and Grants: AMCRC grant number 2.3.4
Date Deposited: 31 Mar 2017 01:47
FoR Codes: 32 BIOMEDICAL AND CLINICAL SCIENCES > 3206 Medical biotechnology > 320699 Medical biotechnology not elsewhere classified @ 20%
31 BIOLOGICAL SCIENCES > 3106 Industrial biotechnology > 310699 Industrial biotechnology not elsewhere classified @ 80%
SEO Codes: 86 MANUFACTURING > 8608 Human Pharmaceutical Products > 860803 Human Pharmaceutical Treatments (e.g. Antibiotics) @ 100%
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