Analysis of hepatitis C virus core protein interaction domains.

Abstract

Hepatitis C virus (HCV) core protein forms the internal viral coat that encapsidates the genomic RNA and is enveloped in a host cell-derived lipid membrane. As the single capsid protein, core should be capable of multimerization but attempts to produce virus-like particles following expression of HCV structural proteins have not been successful. In this study, we have analysed the interaction capacity of full-length and truncated HCV core using the yeast two-hybrid system. Full-length core containing or lacking the translocation signal for the E1 glycoprotein did not interact with full-length or truncated core proteins. Truncation to the N-terminal 122 aa revealed an interaction domain which was mapped to the tryptophan-rich sequence from aa 82-102 and was termed the main homotypic interaction domain. The C-terminal hydrophobic

Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates

“…4, 1999 typic interaction but is involved in weak intramolecular interactions that may mask in cis the homotypic domain in the full-length protein. 52 Host factors may bind to the core protein and acting with ER endopeptidase, release a core protein that is able to multimerize and form the nucleocapsid. In this context, the sensorgram we obtained allowed us to calculate a stoichiometry of 1:7 with 1 molecule of apoAII reacting with 7 molecules of HCV core.…”

“…All constructs were made in pAS2 vector as fusion with the DNA binding domain of the Gal4 yeast transactivator, as previously described. 52 Plasmid pAS-194 encodes full-length core including the signal sequence for translocation of E1 and the first 3 aa of E1. Plasmids pAS-172 to pAS-82 encoded serial Cterminal truncations of the core protein, from which the putative signal peptide of E1 and all or part of the hydrophobic region, were removed.…”

Post-translational Modification of the Hepatitis C Virus Core Protein by Tissue Transglutaminase

“…This higher order structure may be important for the formation of the virions (13,(23)(24)(25)(26). In this report, we demonstrate that a fraction of the HCV core protein dimer is highly stable and cannot be dissociated by boiling in ␤-mercaptoethanol and SDS.…”

Hepatitis c virus and host cell lipids: An intimate connection

“…27 Further cleavage of the signal peptide by signal peptide peptidase, located in the ER membrane ( Fig. 1) is required for mobilization of mature core from the ER to the surface of LDs, which are the presumed sites where nucleocapsid assembly is triggered.…”