Observation of virus-like particles in thin sections of the bleaching scleractinian coral Acropora cytherea

2012 ◽  
Vol 93 (4) ◽  
pp. 909-912 ◽  
Author(s):  
Yvan Bettarel ◽  
Nguyen Thanh Thuy ◽  
Tran Quang Huy ◽  
Phan Kim Hoang ◽  
Thierry Bouvier
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Viral Infection ◽  
Protected Area ◽  
Scleractinian Coral ◽  
Marine Protected Area ◽  
Icosahedral Symmetry ◽  
Thin Sections ◽  
Virus Like Particles ◽  
B Virus

Virus-like particles were observed in thin sections of partially bleaching colonies of the scleractinian Acropora cytherea, collected in the Hon Mun Marine Protected Area (Vietnam). The most common particles were found in the cytoplasm of epidermal cells, exhibiting icosahedral symmetry and measuring 90–140 nm in diameter. Some had a tail-like structure resembling that of certain Hepadnaviridae such as the hepatitis B virus. Some others were tailless with a virion size. Overall, less than 10% of the cells showed obvious signs of infection. Images of virally-parasitized tissues of A. cytherea provide further evidence that corals are a target for viral infection. However, more research is required into their pathogenicity and involvement in bleaching events.

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.

Crystallization of hepatitis B virus core protein shells: determination of cryoprotectant conditions and preliminary X-ray characterization

1999 ◽  
Vol 55 (2) ◽  
pp. 557-560 ◽  
Author(s):  
S. A. Wynne ◽  
A. G. W. Leslie ◽  
P. J. G. Butler ◽  
R. A. Crowther
Keyword(s):  
Hepatitis B Virus ◽  
Nucleic Acid ◽  
Hepatitis B ◽  
Inner Core ◽  
Core Protein ◽  
Sub Saharan Africa ◽  
Icosahedral Symmetry ◽  
Nucleic Acid Binding ◽  
Cell Parameters ◽  
B Virus

Hepatitis B virus causes liver cirrhosis and hepatocellular cancer and is a major cause of death, particularly in Asia and sub-Saharan Africa. The virus consists of an inner core or nucleocapsid, which encloses the viral nucleic acid, with an outer lipid envelope containing surface-antigen proteins. The core protein, when expressed in E. coli, assembles into spherical shells containing 180 or 240 subunits, arranged with T = 3 or T = 4 icosahedral symmetry. The C-terminal region of the protein is involved in nucleic acid binding, and deletion of this region does not prevent capsid formation. C-terminally deleted hepatitis B core shells containing 240 subunits have been crystallized and data has been collected to 3.6 Å resolution from frozen crystals, using butanediol as a cryoprotectant. The crystals have C2 symmetry, with unit-cell parameters a = 538.0, b = 353.0, c = 369.6 Å, β = 132.3°.

Dual-Antigen-Loaded Hepatitis B Virus Core Antigen Virus-like Particles Stimulate Efficient Immunotherapy Against Melanoma

2020 ◽  
Vol 12 (48) ◽  
pp. 53682-53690
Author(s):  
Keman Cheng ◽  
Tao Du ◽  
Yao Li ◽  
Yingqiu Qi ◽  
Huan Min ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Core Antigen ◽  
Virus Like Particles ◽  
Virus Core ◽  
B Virus

Hepatitis B virus-like particles expressing Plasmodium falciparum epitopes induce complement-fixing antibodies against the circumsporozoite protein

Vaccine ◽  
2019 ◽  
Vol 37 (12) ◽  
pp. 1674-1684 ◽  
Author(s):  
Natalie J. Kingston ◽  
Liriye Kurtovic ◽  
Renae Walsh ◽  
Carina Joe ◽  
George Lovrecz ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Circumsporozoite Protein ◽  
Virus Like Particles ◽  
B Virus

scholarly journals Phase I Testing of a Malaria Vaccine Composed of Hepatitis B Virus Core Particles Expressing Plasmodium falciparum Circumsporozoite Epitopes

2004 ◽  
Vol 72 (11) ◽  
pp. 6519-6527 ◽  
Author(s):  
Elizabeth H. Nardin ◽  
Giane A. Oliveira ◽  
J. Mauricio Calvo-Calle ◽  
Kristiane Wetzel ◽  
Carolin Maier ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Phase I ◽  
Malaria Vaccine ◽  
Vaccine Candidate ◽  
Virus Like Particles ◽  
Virus Core ◽  
B Virus ◽  
Malaria Vaccine Candidate

ABSTRACT We report the first phase I trial to assess the safety and immunogenicity of a malaria vaccine candidate, ICC-1132 (Malarivax), composed of a modified hepatitis B virus core protein (HBc) containing minimal epitopes of the Plasmodium falciparum circumsporozoite (CS) protein. When expressed in Escherichia coli, the recombinant ICC-1132 protein forms virus-like particles that were found to be highly immunogenic in preclinical studies of mice and monkeys. Twenty healthy adult volunteers received a 20- or a 50-μg dose of alum-adsorbed ICC-1132 administered intramuscularly at 0, 2, and 6 months. The majority of volunteers in the group receiving the 50-μg dose developed antibodies to CS repeats as well as to HBc. Malaria-specific T cells that secreted gamma interferon were also detected after a single immunization with ICC-1132-alum. These studies support ICC-1132 as a promising malaria vaccine candidate for further clinical testing using more-potent adjuvant formulations and confirm the potential of modified HBc virus-like particles as a delivery platform for vaccines against other human pathogens.

Hepatitis B Virus Core Variants Modify Natural Course of Viral Infection and Hepatocellular Carcinoma Progression

2009 ◽  
Vol 137 (5) ◽  
pp. 1687-1697 ◽  
Author(s):  
Feng–Yu Sung ◽  
Chun–Ming Jung ◽  
Chih–Feng Wu ◽  
Chih–Lin Lin ◽  
Chun–Jen Liu ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Viral Infection ◽  
Natural Course ◽  
Virus Core ◽  
B Virus

scholarly journals An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles

2015 ◽  
Vol 189 (2) ◽  
pp. 73-80 ◽  
Author(s):  
Richard McGonigle ◽  
Wei Boon Yap ◽  
Swee Tin Ong ◽  
Derek Gatherer ◽  
Saskia E. Bakker ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Core Protein ◽  
Virus Like Particles ◽  
Virus Core ◽  
B Virus
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