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J Virol, May 1998, p. 3691-3697, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Hepatitis C Virus Core Protein Binds to the Cytoplasmic Domain of Tumor Necrosis Factor (TNF) Receptor 1 and Enhances TNF-Induced Apoptosis

Nongliao Zhu,1 Ali Khoshnan,2 Robert Schneider,2 Masayuki Matsumoto,2 Gunther Dennert,1 Carl Ware,3 and Michael M. C. Lai1,2,*

Department of Molecular Microbiology and Immunology1 and Howard Hughes Medical Institute,2 University of Southern California School of Medicine, Los Angeles, California 90033, and La Jolla Institute for Allergy and Immunology, San Diego, California 921213

Received 26 November 1997/Accepted 28 January 1998

The hepatitis C virus (HCV) core protein is known to be a multifunctional protein, besides being a component of viral nucleocapsids. Previously, we have shown that the core protein binds to the cytoplasmic domain of lymphotoxin beta  receptor, which is a member of tumor necrosis factor receptor (TNFR) family. In this study, we demonstrated that the core protein also binds to the cytoplasmic domain of TNFR 1. The interaction was demonstrated both by glutathione S-transferase fusion protein pull-down assay in vitro and membrane flotation method in vivo. Both the in vivo and in vitro binding required amino acid residues 345 to 407 of TNFR 1, which corresponds to the "death domain" of this receptor. We have further shown that stable expression of the core protein in a mouse cell line (BC10ME) or human cell lines (HepG2 and HeLa cells) sensitized them to TNF-induced apoptosis, as determined by the TNF cytotoxicity or annexin V apoptosis assay. The presence of the core protein did not alter the level of TNFR 1 mRNA in the cells or expression of TNFR 1 on the cell surface, suggesting that the sensitization of cells to TNF by the viral core protein was not due to up-regulation of TNFR 1. Furthermore, we observed that the core protein blocked the TNF-induced activation of RelA/NF-kappa B in murine BC10ME cells, thus at least partially accounting for the increased sensitivity of BC10ME cells to TNF. However, NF-kappa B activation was not blocked in core protein-expressing HeLa or HepG2 cells, implying another mechanism of TNF sensitization by core protein. These results together suggest that the core protein can promote cell death during HCV infection via TNF signaling pathways possibly as a result of its interaction with the cytoplasmic tail of TNFR 1. Therefore, TNF may play a role in HCV pathogenesis.

* Corresponding author. Mailing address: Department of Molecular Microbiology and Immunology, University of Southern California School of Medicine, 2011 Zonal Ave., HMR-401, Los Angeles, CA 90033-1054. Phone: (213) 342-1748. Fax: (213) 342-9555. E-mail: michlai{at}hsc.usc.edu.

J Virol, May 1998, p. 3691-3697, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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