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Originally published In Press as doi:10.1074/jbc.M102502200 on August 20, 2001

J. Biol. Chem., Vol. 276, Issue 43, 39765-39771, October 26, 2001
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Interferon-kappa , a Novel Type I Interferon Expressed in Human Keratinocytes*

David W. LaFleur, Bernardetta Nardelli, Tatiana Tsareva, Don Mather, Ping Feng, Mark Semenuk, Kara Taylor, Markus Buergin, Diana Chinchilla, Viktor Roshke, Guoxian Chen, Steven M. Ruben, Paula M. PithaDagger , Timothy A. Coleman, and Paul A. Moore§

From Human Genome Sciences, Rockville, Maryland 20850 and Dagger  Department of Oncology, The Johns Hopkins University, Baltimore, Maryland 21231

High throughput cDNA sequencing has led to the identification of interferon-kappa , a novel subclass of type I interferon that displays ~30% homology to other family members. Interferon-kappa consists of 207 amino acids, including a 27-amino acid signal peptide and a series of cysteines conserved in type I interferons. The gene encoding interferon-kappa is located on the short arm of chromosome 9 adjacent to the type I interferon gene cluster and is selectively expressed in epidermal keratinocytes. Expression of interferon-kappa is significantly enhanced in keratinocytes upon viral infection, upon exposure to double-stranded RNA, or upon treatment with either interferon-gamma or interferon-beta . Administration of interferon-kappa recombinant protein imparts cellular protection against viral infection in a species-specific manner. Interferon-kappa activates the interferon-stimulated response element signaling pathway and a panel of genes similar to those regulated by other type I interferons including anti-viral mediators and transcriptional regulators. An antibody that neutralizes the type I interferon receptor completely blocks interferon-kappa signaling, demonstrating that interferon-kappa utilizes the same receptor as other type I interferons. Interferon-kappa therefore defines a novel subclass of type I interferon that is expressed in keratinocytes and expands the repertoire of known proteins mediating host defense.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

 The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF315688, AF384048, and AF384047.

§ To whom correspondence should be addressed: Human Genome Sciences, 9410 Key West Ave., Rockville, MD 20850. Tel.: 301-610-5790 (Ext. 2026); Fax: 301-340-7159; E-mail: paul_moore@hgsi.com.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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