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Published Online: 13 September 2010

Interferon-Lambda: A New Addition to an Old Family

Publication: Journal of Interferon & Cytokine Research
Volume 30, Issue Number 8

Abstract

The discovery and initial description of the interferon-λ (IFN-λ) family in early 2003 opened an exciting new chapter in the field of IFN research. There are 3 IFN-λ genes that encode 3 distinct but highly related proteins denoted IFN-λ1, -λ2, and -λ3. These proteins are also known as interleukin-29 (IL-29), IL-28A, and IL-28B, respectively. Collectively, these 3 cytokines comprise the type III subset of IFNs. They are distinct from both type I and type II IFNs for a number of reasons, including the fact that they signal through a heterodimeric receptor complex that is different from the receptors used by type I or type II IFNs. Although type I IFNs (IFN-α/β) and type III IFNs (IFN-λ) signal via distinct receptor complexes, they activate the same intracellular signaling pathway and many of the same biological activities, including antiviral activity, in a wide variety of target cells. Consistent with their antiviral activity, expression of the IFN-λ genes and their corresponding proteins is inducible by infection with many types of viruses. Therefore, expression of the type III IFNs (IFN-λs) and their primary biological activity are very similar to the type I IFNs. However, unlike IFN-α receptors which are broadly expressed on most cell types, including leukocytes, IFN-λ receptors are largely restricted to cells of epithelial origin. The potential clinical importance of IFN-λ as a novel antiviral therapeutic agent is already apparent. In addition, preclinical studies by several groups indicate that IFN-λ may also be useful as a potential therapeutic agent for other clinical indications, including certain types of cancer.

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Published In

cover image Journal of Interferon & Cytokine Research
Journal of Interferon & Cytokine Research
Volume 30Issue Number 8August 2010
Pages: 555 - 564
PubMed: 20712453

History

Published online: 13 September 2010
Published in print: August 2010
Accepted: 7 July 2010
Received: 7 July 2010

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Raymond P. Donnelly
Division of Therapeutic Proteins, Center for Drug Evaluation and Research, Food and Drug Administration, Bethesda, Maryland.
Sergei V. Kotenko
Department of Biochemistry and Molecular Biology, University Hospital Cancer Center, University of Medicine and Dentistry of New Jersey (UMDNJ), Newark, New Jersey.

Notes

Address correspondence to:Dr. Raymond P. DonnellyDivision of Therapeutic ProteinsCenter for Drug Evaluation and ResearchFood and Drug AdministrationBuilding 29A, Room 3B1529 Lincoln DriveBethesda, MD 20892E-mail: [email protected]
Or
Dr. Sergei KotenkoDepartment of Biochemistry and Molecular BiologyUniversity Hospital Cancer CenterUniversity of Medicine and Dentistry of New Jersey (UMDNJ)185 South Orange Av.Newark, NJ 07103E-mail: [email protected]

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No competing financial interests exist.

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