Post-translational modification of the hepatitis C virus core protein by tissue transglutaminase

The Journal of Biological Chemistry
W LuJ H Ou Jh

Abstract

The hepatitis C virus (HCV) core protein is a structural protein that packages the viral genomic RNA. In this study, we demonstrate that a stable core protein dimer could be produced in liver cells. The production of this protein could be enhanced by calphostin C and serum deprivation. This protein was determined to be the core protein dimer because of its reactivity with the anti-core antibody, its similar electrophoretic mobility compared with that of the core protein dimer generated by cross-linking with glutaraldehyde, and its increase in size by a hemagglutinin tag fused to the core protein sequence. This core protein dimer was highly stable and resistant to SDS and beta-mercaptoethanol. The enzyme that mediated the formation of this stable core protein dimer was determined to be the tissue transglutaminase (tTG) because, first, tTG could be activated by calphostin C and serum deprivation; second, the formation of this dimer was suppressed by monodansylcadaverine, a tTG inhibitor; and third, the core protein could be cross-linked by tTG in vitro. Thus, the HCV core protein represents the first known viral structural protein substrate of tTG. The post-translational modification by tTG reduced the RNA binding activity of the...Continue Reading

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Citations

Dec 23, 2004·Journal of Virology·Ryosuke SuzukiTetsuro Suzuki
Oct 31, 2008·Journal of Virology·Kamile YuksekJing-Hsiung James Ou
Jul 4, 2008·Amino Acids·Angelo Facchiano, Francesco Facchiano
Feb 4, 2003·Nature Reviews. Molecular Cell Biology·Laszlo Lorand, Robert M Graham
Mar 29, 2011·Modern Pathology : an Official Journal of the United States and Canadian Academy of Pathology, Inc·Franca Del NonnoLaura Falasca

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