Functional characterization of the interaction between human La and hepatitis B virus RNA.
The La protein is a multifunctional RNA-binding protein and has also been suggested to be involved in the stabilization of hepatitis B virus (HBV) RNA. Here we demonstrate that antibodies against the human La protein specifically precipitate HBV RNA from HBV ribonucleoprotein-containing mammalian cell extracts, providing evidence for the association between human La and HBV RNA. Moreover, we report that the turnover of HBV RNA depends on structural features and less on the primary sequence of the La-binding site on the viral RNA. In addition we show that the interaction between human La and HBV RNA in vitro is modulated by accessory factor(s) in a phosphorylation-dependent manner. Taken together these data indicate that both structural features, the composition of La/HBV ribonucleoprotein particles as well as interacting cellular factors, are critical determinants in the regulation of the stability of the HBV RNA.
Ehlers
Imke
I
Heinrich-Pette Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, Martinistrasse 52, D-20251, Germany.
Horke
Sven
S
Reumann
Kerstin
K
Rang
Andreas
A
Grosse
Frank
F
Will
Hans
H
Heise
Tilman
T
D019943:Amino Acid Substitution; D001324:Autoantigens / Q000502:physiology*; D001483:Base Sequence; D017931:DNA Primers; D004279:DNA, Viral / Q000235:genetics; D005838:Genotype; D006207:Half-Life; D006515:Hepatitis B virus / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D020641:Polymorphism, Single Nucleotide; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015183:Restriction Mapping; D012261:Ribonucleoproteins / Q000378:metabolism / Q000502:physiology*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D000097585:SS-B Antigen
D001324:Autoantigens; D017931:DNA Primers; D004279:DNA, Viral; D012367:RNA, Viral; D012261:Ribonucleoproteins; D000097585:SS-B Antigen