scholarly journals The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function

1993 ◽  
Vol 21 (17) ◽  
pp. 3967-3975 ◽  
Author(s):  
Thomas Knaus ◽  
Michael Nassal
1999 ◽  
Vol 73 (7) ◽  
pp. 5767-5776 ◽  
Author(s):  
Tilman Heise ◽  
Luca G. Guidotti ◽  
Francis V. Chisari

ABSTRACT We recently identified three nuclear proteins (p45, p39, and p26) that bind to a 91-nucleotide (nt) RNA element between nt 1243 and 1333 in hepatitis B virus (HBV) RNA, and we showed that these proteins and HBV RNA are regulated coordinately by gamma interferon and tumor necrosis factor alpha. Purification and sequence analysis of tryptic peptides obtained from p39 revealed sequence homology to the mouse La protein. Immunoprecipitation experiments showed that p45, p39, and p26 were recognized by anti-La-specific antiserum, indicating that p45 is the full-length La protein and that p39 and p26 are likely to be proteolytic La cleavage products. Furthermore, in competition experiments we found that all three La proteins bind, in a phosphorylation-dependent manner, to the same predicted stem-loop structure located between nt 1275 and 1291 of HBV, withKd s of approximately 1.0 nM. Collectively, these results support the notion that the La protein may contribute to HBV RNA stability, constitutively and in response to inflammatory cytokines.


2006 ◽  
Vol 34 (16) ◽  
pp. 4449-4457 ◽  
Author(s):  
Sara Flodell ◽  
Michael Petersen ◽  
Frederic Girard ◽  
Janusz Zdunek ◽  
Karin Kidd-Ljunggren ◽  
...  

2002 ◽  
Vol 147 (3) ◽  
pp. 471-491 ◽  
Author(s):  
H. J. Shin ◽  
S. S. Kim ◽  
Y. H. Cho ◽  
S. G. Lee ◽  
H. M. Rho

PLoS ONE ◽  
2011 ◽  
Vol 6 (11) ◽  
pp. e27862 ◽  
Author(s):  
Hui Feng ◽  
Jürgen Beck ◽  
Michael Nassal ◽  
Kang-hong Hu

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