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.
Heinrich-Pette Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, Martinistrasse 52, D-20251, Germany.
Imke
I
Ehlers
Sven
S
Horke
Kerstin
K
Reumann
Andreas
A
Rang
Frank
F
Grosse
Hans
H
Will
Tilman
T
Heise
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