scholarly journals Construction and Immunological Evaluation of Multivalent Hepatitis B Virus (HBV) Core Virus-Like Particles Carrying HBV and HCV Epitopes

2010 ◽  
Vol 17 (6) ◽  
pp. 1027-1033 ◽  
Author(s):  
Irina Sominskaya ◽  
Dace Skrastina ◽  
Andris Dislers ◽  
Denis Vasiljev ◽  
Marija Mihailova ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Antibody Response ◽  
T Cell Activation ◽  
Cell Activation ◽  
Cytotoxic T Lymphocyte ◽  
High Titer ◽  
Virus Like Particles ◽  
Chimeric Vlps ◽  
B Virus

ABSTRACT A multivalent vaccine candidate against hepatitis B virus (HBV) and hepatitis C virus (HCV) infections was constructed on the basis of HBV core (HBc) virus-like particles (VLPs) as carriers. Chimeric VLPs that carried a virus-neutralizing HBV pre-S1 epitope corresponding to amino acids (aa) 20 to 47 in the major immunodominant region (MIR) and a highly conserved N-terminal HCV core epitope corresponding to aa 1 to 60 at the C terminus of the truncated HBcΔ protein (N-terminal aa 1 to 144 of full-length HBc) were produced in Escherichia coli cells and examined for their antigenicity and immunogenicity. The presence of two different foreign epitopes within the HBc molecule did not interfere with its VLP-forming ability, with the HBV pre-S1 epitope exposed on the surface and the HCV core epitope buried within the VLPs. After immunization of BALB/c mice, specific T-cell activation by both foreign epitopes and a high-titer antibody response against the pre-S1 epitope were found, whereas an antibody response against the HBc carrier was notably suppressed. Both inserted epitopes also induced a specific cytotoxic-T-lymphocyte (CTL) response, as shown by the gamma interferon (IFN-γ) production profile.

Hepatitis B virus antigen-specific T-cell activation in patients with acute and chronic hepatitis B

1991 ◽  
Vol 13 (3) ◽  
pp. 310-317 ◽  
Author(s):  
M.-C. Jung ◽  
U. Spengler ◽  
W. Schraut ◽  
R. Hoffmann ◽  
R. Zachoval ◽  
...  
Keyword(s):  
Chronic Hepatitis ◽  
Hepatitis B Virus ◽  
T Cell ◽  
Hepatitis B ◽  
Chronic Hepatitis B ◽  
T Cell Activation ◽  
Cell Activation ◽  
Virus Antigen ◽  
B Virus ◽  
Acute And Chronic Hepatitis

scholarly journals The Hepatitis B Virus X Protein Induces HIV-1 Replication and Transcription in Synergy with T-cell Activation Signals

2001 ◽  
Vol 276 (38) ◽  
pp. 35435-35443 ◽  
Author(s):  
Marta Gómez-Gonzalo ◽  
Marta Carretero ◽  
Joaquı́n Rullas ◽  
Enrique Lara-Pezzi ◽  
José Aramburu ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
T Cell ◽  
Hepatitis B ◽  
T Cell Activation ◽  
Cell Activation ◽  
X Protein ◽  
B Virus ◽  
Hiv 1

scholarly journals Efficient Production of Chimeric Hepatitis B Virus-Like Particles Bearing an Epitope of Hepatitis E Virus Capsid by Transient Expression in Nicotiana benthamiana

Life ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 64
Author(s):  
Gergana Zahmanova ◽  
Milena Mazalovska ◽  
Katerina Takova ◽  
Valentina Toneva ◽  
Ivan Minkov ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Nicotiana Benthamiana ◽  
Hepatitis E Virus ◽  
Chimeric Protein ◽  
Hepatitis E ◽  
Core Antigen ◽  
Efficient Production ◽  
Virus Like Particles ◽  
B Virus

The core antigen of hepatitis B virus (HBcAg) is capable of self-assembly into virus-like particles (VLPs) when expressed in a number of heterologous systems. Such VLPs are potential carriers of foreign antigenic sequences for vaccine design. In this study, we evaluated the production of chimeric HBcAg VLPs presenting a foreign epitope on their surface, the 551–607 amino acids (aa) immunological epitope of the ORF2 capsid protein of hepatitis E virus. A chimeric construct was made by the insertion of 56 aa into the immunodominant loop of the HBcAg. The sequences encoding the chimera were inserted into the pEAQ-HT vector and infiltrated into Nicotiana benthamiana leaves. The plant-expressed chimeric HBcHEV ORF2 551–607 protein was recognized by an anti-HBcAg mAb and anti-HEV IgG positive swine serum. Electron microscopy showed that plant-produced chimeric protein spontaneously assembled into “knobbly” ~34 nm diameter VLPs. This study shows that HBcAg is a promising carrier platform for the neutralizing epitopes of hepatitis E virus (HEV) and the chimeric HBcAg/HEV VLPs could be a candidate for a bivalent vaccine.

scholarly journals Efficient Generation of a Hepatitis B Virus Cytotoxic T Lymphocyte Epitope Requires the Structural Features of Immunoproteasomes

2000 ◽  
Vol 191 (3) ◽  
pp. 503-514 ◽  
Author(s):  
Alice J.A.M. Sijts ◽  
Thomas Ruppert ◽  
Barbara Rehermann ◽  
Marion Schmidt ◽  
Ulrich Koszinowski ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Structural Features ◽  
Core Antigen ◽  
Ctl Epitope ◽  
Cleavage Specificity ◽  
B Virus ◽  
Ifn Γ

Interferon (IFN)-γ–induced cells express the proteasome subunits low molecular weight protein (LMP)2, LMP7, and MECL-1 (multicatalytic endopeptidase complex–like 1), leading to the formation of immunoproteasomes. Although these subunits are thought to optimize MHC class I antigen processing, the extent of their role and the mechanistic aspects involved remain unclear. Herein, we study the proteolytic generation of an human histocompatibility leukocyte antigen (HLA)-Aw68–restricted hepatitis B virus core antigen (HBcAg) cytotoxic T lymphocyte (CTL) epitope that is recognized by peripheral blood lymphocytes from patients with acute self-limited but not chronic hepatitis B virus (HBV). Immunological data suggest that IFN-γ–induced rather than uninduced HeLa cells process and present the HBV CTL epitope upon infection with HBcAg-expressing vaccinia viruses. Analyses of 20S proteasome digests of synthetic polypeptides covering the antigenic HBcAg peptide demonstrate that only immunoproteasomes efficiently perform the cleavages needed for the liberation of this HBV CTL epitope. Although the concerted presence of the three immunosubunits appears essential, we find that both catalytically active LMP7 and inactive LMP7 T1A support CTL epitope generation. We conclude that LMP7 influences the structural features of 20S proteasomes, thereby enhancing the activity of the LMP2 and MECL-1 catalytic sites, which provide cleavage specificity. Thus, LMP7 incorporation is of greater functional importance for the generation of an HBV CTL epitope than cleavage specificity.

Is antigenic variability a strategy adopted by hepatitis B virus to escape cytotoxic T-lymphocyte surveillance?

1996 ◽  
Vol 7 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Carlo Ferrari ◽  
Antonio Bertoletti ◽  
Franco Fiaccadori ◽  
Francis V. Chisari*
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Antigenic Variability ◽  
B Virus
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