scholarly journals Translation of hepatitis B virus (HBV) surface proteins from the HBV pregenome and precore RNAs in Semliki Forest virus-driven expression

2004 ◽  
Vol 85 (11) ◽  
pp. 3343-3351 ◽  
Author(s):  
Anna Zajakina ◽  
Tatyana Kozlovska ◽  
Ruta Bruvere ◽  
Jekaterina Aleksejeva ◽  
Paul Pumpens ◽  
...  

Hepatitis B virus (HBV) pregenome RNA (pgRNA) serves as a translation template for the HBV core (HBc) protein and viral polymerase (Pol). HBV precore RNA (pcRNA) directs the synthesis of the precore (preC) protein, a precursor of the hepatitis B e antigen (HBeAg). pgRNA and pcRNA were expressed in the Semliki Forest virus (SFV) expression system. Besides the HBc and preC proteins, there was revealed the synthesis of all three forms of HBV surface (HBs) proteins: long (LHBs), middle (MHBs) and short (SHBs), the start codons of which are located more than 1000 nt downstream of the HBc and preC start codons. Moreover, other HBV templates, such as 3′-truncated pgRNA lacking 3′ direct repeat and Pol mRNA, both carrying internally the HBs sequences, provided the synthesis of three HBs protein forms in the SFV-driven expression system. Maximal production of the HBs was provided by Pol mRNA, while HBc- and preC-producing templates showed relatively low internal translation of the HBs. These data allow the proposal of a ribosome leaky scanning model of internal translation initiation for HBs proteins. The putative functional role of such exceptional synthesis of the HBs proteins from the pgRNA and pcRNA templates in the natural HBV infection process needs further evaluation.

1986 ◽  
Vol 6 (5) ◽  
pp. 1393-1400
Author(s):  
M J Roossinck ◽  
S Jameel ◽  
S H Loukin ◽  
A Siddiqui

We studied the expression of the core region of the hepatitis B virus genome in mammalian cells with recombinant plasmid vectors. Stably transformed rat fibroblast cell lines were established by transfection with vectors containing subgenomic and genome-length hepatitis B virus DNA, followed by G418 selection. The RNA transcripts directed by the core region were characterized by Northern blot hybridization and S1 nuclease mapping. Using the chloramphenicol acetyltransferase gene expression system, the promoter activity located upstream of the core open reading frame was confirmed. The synthesis of core and e polypeptides was studied with a commercial radioimmunoassay. These studies show that partial deletion of the precore sequences abolished secretion of the e antigen, but there was pronounced synthesis of the core antigen in transfected cells.


2011 ◽  
Vol 26 (2) ◽  
pp. 131-138 ◽  
Author(s):  
Jian Qiu ◽  
Bo Qin ◽  
Simon Rayner ◽  
Chun-chen Wu ◽  
Rong-juan Pei ◽  
...  

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 1023 ◽  
Author(s):  
Modhusudon Shaha ◽  
Palash Kumar Sarker ◽  
Md. Saddam Hossain ◽  
Keshob Chandra Das ◽  
Munira Jahan ◽  
...  

The burden of chronic hepatitis B virus (HBV) infections is increasingly detected nowadays. Herein, we report a complete genome of HBV subgenotype C2 (HBV/C2) from a HBV infected patient. Complete genome analysis revealed that the isolated strain was a non-recombinant wild type and had several regular substitutions in the reverse transcriptase domain and small surface proteins of HBV. This study may help clinicians and scientists gain in-depth knowledge on the current substitutions of HBV/C2 genome and to identify potential therapies against HBV infections.


2021 ◽  
Vol 118 (17) ◽  
pp. e2022464118
Author(s):  
Lauriane Lecoq ◽  
Shishan Wang ◽  
Marie Dujardin ◽  
Peter Zimmermann ◽  
Leonard Schuster ◽  
...  

Viral hepatitis is growing into an epidemic illness, and it is urgent to neutralize the main culprit, hepatitis B virus (HBV), a small-enveloped retrotranscribing DNA virus. An intriguing observation in HB virion morphogenesis is that capsids with immature genomes are rarely enveloped and secreted. This prompted, in 1982, the postulate that a regulated conformation switch in the capsid triggers envelopment. Using solid-state NMR, we identified a stable alternative conformation of the capsid. The structural variations focus on the hydrophobic pocket of the core protein, a hot spot in capsid–envelope interactions. This structural switch is triggered by specific, high-affinity binding of a pocket factor. The conformational change induced by the binding is reminiscent of a maturation signal. This leads us to formulate the “synergistic double interaction” hypothesis, which explains the regulation of capsid envelopment and indicates a concept for therapeutic interference with HBV envelopment.


PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e90608 ◽  
Author(s):  
Yuri Churin ◽  
Martin Roderfeld ◽  
Johannes Stiefel ◽  
Tilman Würger ◽  
Dirk Schröder ◽  
...  

1990 ◽  
Vol 98 (4) ◽  
pp. 1017-1023 ◽  
Author(s):  
Hans P. Dienes ◽  
Wolfram H. Gerlich ◽  
Marita Wörsdörfer ◽  
Guido Gerken ◽  
Leonardo Bianchi ◽  
...  

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