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J. Biol. Chem., Vol. 280, Issue 48, 39802-39808, December 2, 2005

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Hepatitis C Virus Nonstructural Proteins Inhibit Apolipoprotein B100 Secretion^*

Angela M. Domitrovich1, Daniel J. Felmlee, and Aleem Siddiqui2

From the Department of Medicine, Moores Cancer Center, University of California at San Diego, La Jolla, California 92093-0803 and the Program in Molecular Biology, Department of Microbiology, University of Colorado Health Sciences Center, Aurora, Colorado 80045

Host genes involved in lipid metabolism are differentially regulated during the early stages of hepatitis C virus (HCV) infection. The majority of lipids synthesized in the liver are exported to other tissues in the form of lipoproteins. The formation of these lipoproteins is dependent upon the association of triglycerides with apolipoprotein B100. Using the HCV subgenomic replicon expression system, we show that secretion of apoB100 is significantly reduced. Inhibition of apoB100 degradation by ALLN did not improve secretion. Triglyceride levels as well as microsomal triglyceride transfer protein mRNA and activity levels were reduced in replicon-expressing cells, indicating potential reasons for the observed decrease. Further evidence is presented for the interaction between the HCV nonstructural protein 5A and apoB100. These results provide further insight into the alteration of lipid metabolism by HCV.

Received for publication, September 21, 2005

^* This work is supported by an National Institutes of Health Grant DK061566 (to A. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by the W. M. Thorkildsen Research Award.

² To whom correspondence should be addressed. Tel.: 858-822-1750; Fax: 858-822-1749; E-mail: asiddiqui{at}ucsd.edu.

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