HCV core protein modulates the immune response against the HBV surface antigen in mice

2003 ◽  
Vol 310 (1) ◽  
pp. 59-63 ◽  
Author(s):  
Julio C Aguilar ◽  
Nelson Acosta-Rivero ◽  
Santiago Dueñas-Carrera ◽  
Juan Morales Grillo ◽  
Dagmara Pichardo ◽  
...  
Keyword(s):  
Immune Response ◽  
Surface Antigen ◽  
Core Protein ◽  
Hcv Core Protein

scholarly journals Inhibition of the HCV Core Protein on the Immune Response to HBV Surface Antigen and on HBV Gene Expression and Replication In Vivo

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e45146 ◽  
Author(s):  
Wenbo Zhu ◽  
Chunchen Wu ◽  
Wanyu Deng ◽  
Rongjun Pei ◽  
Yun Wang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Immune Response ◽  
Surface Antigen ◽  
Core Protein ◽  
Hcv Core Protein

A truncated HCV core protein elicits a potent immune response with a strong participation of cellular immunity components in mice

Vaccine ◽  
2001 ◽  
Vol 19 (28-29) ◽  
pp. 3940-3946 ◽  
Author(s):  
Julio César Alvarez-Obregón ◽  
Santiago Dueñas-Carrera ◽  
Carmen Valenzuela ◽  
Juan Morales Grillo
Keyword(s):  
Immune Response ◽  
Cellular Immunity ◽  
Core Protein ◽  
Hcv Core Protein ◽  
Potent Immune Response

M1809 Natural Killer Cells Target HCV Core Protein in Naïve Immune Response in HCV Transgenic Mice

2009 ◽  
Vol 136 (5) ◽  
pp. A-843
Author(s):  
Satoh Kenichi ◽  
Takahashi Hiroki ◽  
Kohara Michinori ◽  
Ohkusa Toshifumi ◽  
Zeniya Mikio ◽  
...  
Keyword(s):  
Immune Response ◽  
Natural Killer Cells ◽  
Transgenic Mice ◽  
Natural Killer ◽  
Core Protein ◽  
Killer Cells ◽  
Hcv Core Protein

scholarly journals HCV Core Protein Induces Chemokine CCL2 and CXCL10 Expression Through NF-κB Signaling Pathway in Macrophages

2021 ◽  
Vol 12 ◽  
Author(s):  
Xiaotian Song ◽  
Xue Gao ◽  
Yadong Wang ◽  
Rameez Raja ◽  
Yaoyu Zhang ◽  
...  
Keyword(s):  
Immune Response ◽  
Viral Infection ◽  
Signaling Pathway ◽  
Innate Immune Response ◽  
Kupffer Cells ◽  
Core Protein ◽  
Innate Immune ◽  
Hcv Infection ◽  
Structural Protein ◽  
Hcv Core Protein

HCV core protein is the first structural protein synthesized during hepatitis C virus (HCV) infection and replication. It is released from virus infected liver cells and mediates multiple functions to affect host cell response. The innate immune response is the first line of defense against viral infection. After HCV infection, Kupffer cells (KCs) which are liver macrophages play an important role in host innate immune response. Kupffer cells act as phagocytes and release different cytokines and chemokines to counter viral infection and regulate inflammation and fibrosis in liver. Earlier, we have demonstrated that HCV core protein interacts with gC1qR and activates MAPK, NF-κB and PI3K/AKT pathways in macrophages. In this study, we explored the effect of HCV core protein on CCL2 and CXCL10 expression in macrophages and the signaling pathways involved. Upon silencing of gC1qR, we observed a significant decrease expression of CCL2 and CXCL10 in macrophages in the presence of HCV core protein. Inhibiting NF-κB pathway, but not P38, JNK, ERK and AKT pathways greatly reduced the expression of CCL2 and CXCL10. Therefore, our results indicate that interaction of HCV core protein with gC1qR could induce CCL2 and CXCL10 secretion in macrophages via NF-κB signaling pathway. These findings may shed light on the understanding of how leukocytes migrate into the liver and exaggerate host-derived immune responses and may provide novel therapeutic targets in HCV chronic inflammation.

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.

scholarly journals Immune response by nasal delivery of hepatitis B surface antigen and codelivery of a CpG ODN in alginate coated chitosan nanoparticles

2008 ◽  
Vol 69 (2) ◽  
pp. 405-416 ◽  
Author(s):  
Olga Borges ◽  
Anabela Cordeiro-da-Silva ◽  
Joana Tavares ◽  
Nuno Santarém ◽  
Adriano de Sousa ◽  
...  
Keyword(s):  
Immune Response ◽  
Hepatitis B ◽  
Surface Antigen ◽  
Hepatitis B Surface Antigen ◽  
Chitosan Nanoparticles ◽  
Nasal Delivery ◽  
Cpg Odn

scholarly journals Analysis of Structures and Epitopes of Surface Antigen Glycoproteins Expressed in Bradyzoites ofToxoplasma gondii

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Hua Cong ◽  
Min Zhang ◽  
Qingli Zhang ◽  
Jing Gong ◽  
Haizi Cong ◽  
...  
Keyword(s):  
Immune Response ◽  
Toxoplasma Gondii ◽  
Immune Responses ◽  
Surface Antigen ◽  
Protein Sequence ◽  
Protozoan Parasite ◽  
3D Models ◽  
Chronic Infections ◽  
Homologous Proteins ◽  
Protein Sequence Alignment

Toxoplasma gondiiis a protozoan parasite capable of infecting humans and animals. Surface antigen glycoproteins, SAG2C, -2D, -2X, and -2Y, are expressed on the surface of bradyzoites. These antigens have been shown to protect bradyzoites against immune responses during chronic infections. We studied structures of SAG2C, -2D, -2X, and -2Y proteins using bioinformatics methods. The protein sequence alignment was performed by T-Coffee method. Secondary structural and functional domains were predicted using software PSIPRED v3.0 and SMART software, and 3D models of proteins were constructed and compared using the I-TASSER server, VMD, and SWISS-spdbv. Our results showed that SAG2C, -2D, -2X, and -2Y are highly homologous proteins. They share the same conserved peptides and HLA-I restricted epitopes. The similarity in structure and domains indicated putative common functions that might stimulate similar immune response in hosts. The conserved peptides and HLA-restricted epitopes could provide important insights on vaccine study and the diagnosis of this disease.

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