scholarly journals Spectroscopic study of conformational changes accompanying self-assembly of HCV core protein

2006 ◽  
Vol 66 (1) ◽  
pp. 110-117 ◽  
Author(s):  
Arantxa Rodríguez-Casado ◽  
Marina Molina ◽  
Pedro Carmona
Keyword(s):  
Spectroscopic Study ◽  
Conformational Changes ◽  
Self Assembly ◽  
Core Protein ◽  
Hcv Core Protein

scholarly journals Nanosized Particles Assembled by a Recombinant Virus Protein Are Able to Encapsulate Negatively Charged Molecules and Structured RNA

Polymers ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 858
Author(s):  
Hemalatha Mani ◽  
Yi-Cheng Chen ◽  
Yen-Kai Chen ◽  
Wei-Lin Liu ◽  
Shih-Yen Lo ◽  
...  
Keyword(s):  
Self Assembly ◽  
Rna Binding ◽  
Core Protein ◽  
Average Diameter ◽  
Virus Protein ◽  
Force Microscopy ◽  
Atomic Force ◽  
Hcv Core Protein

RNA-based molecules have recently become hot candidates to be developed into therapeutic agents. However, successful applications of RNA-based therapeutics might require suitable carriers to protect the RNA from enzymatic degradation by ubiquitous RNases in vivo. Because of their better biocompatibility and biodegradability, protein-based nanoparticles are considered to be alternatives to their synthetic polymer-based counterparts for drug delivery. Hepatitis C virus (HCV) core protein has been suggested to be able to self-assemble into nucleocapsid-like particles in vitro. In this study, the genomic RNA-binding domain of HCV core protein consisting of 116 amino acids (p116) was overexpressed with E. coli for investigation. The recombinant p116 was able to assemble into particles with an average diameter of approximately 27 nm, as visualized by electron microscopy and atomic force microscopy. Measurements with fluorescence spectroscopy, flow cytometry, and fluorescence quenching indicated that the p116-assembled nanoparticles were able to encapsulate small anionic molecules and structured RNA. This study demonstrates methods that exploit the self-assembly nature of a virus-derived protein for nanoparticle production. This study also suggests that the virus-derived protein-assembled particles could possibly be developed into potential carriers for anionic molecular drugs and structured RNA-based therapeutics.

scholarly journals Hepatitis C Virus Core Protein Inhibits Tumor Necrosis Factor Alpha-Mediated Apoptosis by a Protective Effect Involving Cellular FLICE Inhibitory Protein

2006 ◽  
Vol 80 (9) ◽  
pp. 4372-4379 ◽  
Author(s):  
Kousuke Saito ◽  
Keith Meyer ◽  
Rebecca Warner ◽  
Arnab Basu ◽  
Ratna B. Ray ◽  
...  
Keyword(s):  
Tumor Necrosis ◽  
Core Protein ◽  
Death Domain ◽  
Inhibitory Protein ◽  
Necrosis Factor Alpha ◽  
Hcv Core Protein ◽  
Tnf Α ◽  
Factor Alpha ◽  
Domain Protein ◽  
Necrosis Factor

ABSTRACT We have previously shown that hepatitis C virus (HCV) core protein modulates multiple cellular processes, including those that inhibit tumor necrosis factor alpha (TNF-α)-mediated apoptosis. In this study, we have investigated the signaling mechanism for inhibition of TNF-α-mediated apoptosis in human hepatoma (HepG2) cells expressing core protein alone or in context with other HCV proteins. Activation of caspase-3 and the cleavage of DNA repair enzyme poly(ADP-ribose) polymerase were inhibited upon TNF-α exposure in HCV core protein-expressing HepG2 cells. In vivo protein-protein interaction studies displayed an association between TNF receptor 1 (TNFR1) and TNFR1-associated death domain protein (TRADD), suggesting that the core protein does not perturb this interaction. A coimmunoprecipitation assay also suggested that HCV core protein does not interfere with the TRADD-Fas-associated death domain protein (FADD)-procaspase-8 interaction. Further studies indicated that HCV core protein expression inhibits caspase-8 activation by sustaining the expression of cellular FLICE (FADD-like interleukin-1β-converting enzyme)-like inhibitory protein (c-FLIP). Similar observations were also noted upon expression of core protein in context to other HCV proteins expressed from HCV full-length plasmid DNA or a replicon. A decrease in endogenous c-FLIP by specific small interfering RNA induced TNF-α-mediated apoptotic cell death and caspase-8 activation. Taken together, our results suggested that the TNF-α-induced apoptotic pathway is inhibited by a sustained c-FLIP expression associated with the expression of HCV core protein, which may play a role in HCV-mediated pathogenesis.

scholarly journals Differential Effects on the Hepatitis C Virus (HCV) Internal Ribosome Entry Site by Vitamin B12 and the HCV Core Protein

2004 ◽  
Vol 78 (21) ◽  
pp. 12075-12081 ◽  
Author(s):  
Dongsheng Li ◽  
William B. Lott ◽  
John Martyn ◽  
Gholamreza Haqshenas ◽  
Eric J. Gowans
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Internal Ribosome Entry Site ◽  
Core Protein ◽  
Vitamin B ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Hcv Core Protein ◽  
Hcv Ires

ABSTRACT To investigate the role of the hepatitis C virus internal ribosome entry site (HCV IRES) domain IV in translation initiation and regulation, two chimeric IRES elements were constructed to contain the reciprocal domain IV in the otherwise HCV and classical swine fever virus IRES elements. This permitted an examination of the role of domain IV in the control of HCV translation. A specific inhibitor of the HCV IRES, vitamin B12, was shown to inhibit translation directed by all IRES elements which contained domain IV from the HCV and the GB virus B IRES elements, whereas the HCV core protein could only suppress translation from the wild-type HCV IRES. Thus, the mechanisms of translation inhibition by vitamin B12 and the core protein differ, and they target different regions of the IRES.

Raman spectroscopic study of conformational changes in the amorphous phase of poly(lactic acid) during deformation

Polymer ◽  
2004 ◽  
Vol 45 (12) ◽  
pp. 4241-4248 ◽  
Author(s):  
Xiaozhen Yang ◽  
Shuhui Kang ◽  
Yuning Yang ◽  
Kaoru Aou ◽  
Shaw Ling Hsu
Keyword(s):  
Lactic Acid ◽  
Spectroscopic Study ◽  
Amorphous Phase ◽  
Conformational Changes ◽  
Poly Lactic Acid ◽  
Raman Spectroscopic ◽  
Raman Spectroscopic Study

scholarly journals Hepatitis C Virus Core Protein Enhances NF-κB Signal Pathway Triggering by Lymphotoxin-β Receptor Ligand and Tumor Necrosis Factor Alpha

1999 ◽  
Vol 73 (2) ◽  
pp. 1672-1681 ◽  
Author(s):  
Li-Ru You ◽  
Chun-Ming Chen ◽  
Yan-Hwa Wu Lee
Keyword(s):  
Tumor Necrosis Factor ◽  
Hela Cells ◽  
Tumor Necrosis ◽  
Core Protein ◽  
Cell Types ◽  
Necrosis Factor Alpha ◽  
Hcv Core Protein ◽  
Tnf Α ◽  
Β Receptor ◽  
Necrosis Factor

ABSTRACT Our previous study indicated that the core protein of hepatitis C virus (HCV) can associate with tumor necrosis factor receptor (TNFR)-related lymphotoxin-β receptor (LT-βR) and that this protein-protein interaction plays a modulatory effect on the cytolytic activity of recombinant form LT-βR ligand (LT-α1β2) but not tumor necrosis factor alpha (TNF-α) in certain cell types. Since both TNF-α/TNFR and LT-α1β2/LT-βR are also engaged in transcriptional activator NF-κB activation or c-Jun N-terminal kinase (JNK) activation, the biological effects of the HCV core protein on these regards were elucidated in this study. As demonstrated by the electrophoretic mobility shift assay, the expression of HCV core protein prolonged or enhanced the TNF-α or LT-α1β2-induced NF-κB DNA-binding activity in HuH-7 and HeLa cells. The presence of HCV core protein in HeLa or HuH-7 cells with or without cytokine treatment also enhanced the NF-κB-dependent reporter plasmid activity, and this effect was more strongly seen with HuH-7 cells than with HeLa cells. Western blot analysis suggested that this modulation of the NF-κB activity by the HCV core protein was in part due to elevated or prolonged nuclear retention of p50 or p65 species of NF-κB in core protein-producing cells with or without cytokine treatment. Furthermore, the HCV core protein enhanced or prolonged the IκB-β degradation triggering by TNF-α or LT-α1β2 both in HeLa and HuH-7 cells. In contrast to that of IκB-β, the increased degradation of IκB-α occurred only in LT-α1β2-treated core-producing HeLa cells and not in TNF-α-treated cells. Therefore, the HCV core protein plays a modulatory effect on NF-κB activation triggering by both cytokines, though the mechanism of NF-κB activation, in particular the regulation of IκB degradation, is rather cell line and cytokine specific. Studies also suggested that the HCV core protein had no effect on TNF-α-stimulated JNK activity in both HeLa and HuH-7 cells. These findings, together with our previous study, strongly suggest that among three signaling pathways triggered by the TNF-α-related cytokines, the HCV core protein potentiates NF-κB activation in most cell types, which in turn may contribute to the chronically activated, persistent state of HCV-infected cells.

scholarly journals SPECTROSCOPIC STUDY OF THE PROCESS OF HYPOCHROMIC EFFECT IN SOL T IN SOLUTIONS OF N UTIONS OF NATURAL D TURAL DYES AND VI YES AND VITAMIN B2 AMIN B2

2020 ◽  
Vol 4 (3) ◽  
pp. 21-27
Author(s):  
Salikh Khusenovich Astanov ◽  
◽  
Siddiq Kakhkharovich Kakhkharov ◽  
Keyword(s):  
Spectroscopic Study ◽  
Binary Mixtures ◽  
Self Assembly ◽  
Spectroscopic Method ◽  
Dipole Interaction ◽  
Absorption Capacity ◽  
Vitamin B2 ◽  
Intense Absorption ◽  
Hypochromic Effect

The process of self-assembly of riboflavin molecules in aqueous and binary mixtures of solvents was investigated by the spectroscopic method. It was shown that during the assembly of vitamin B2 molecules, dipole-dipole interaction occurs, as a result of which resonant splitting of excited electronic levels of riboflavin molecules occurs. And the observable hypo chromic effect is due to a decrease in the intense absorption capacity of the aggregated riboflavin molecules themselves.

Hepatitis C virus (HCV) core protein enhances the immunogenicity of a co-delivered DNA vaccine encoding HCV structural antigens in mice

2006 ◽  
Vol 44 (1) ◽  
pp. 9 ◽  
Author(s):  
Marleny González ◽  
Liz Alvarez-Lajonchere ◽  
Julio César Alvarez-Obregón ◽  
Ivis Guerra ◽  
Ariel Viña ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Dna Vaccine ◽  
Core Protein ◽  
Hcv Core Protein
Sign in / Sign up

Export Citation Format

Share Document