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La autoantigen specifically recognizes a predicted stem-loop in hepatitis B virus RNA

Academic Article
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Overview

authors

  • Heise, T.
  • Guidotti, Luca
  • Chisari, Francis

publication date

  • July 1999

journal

  • Journal of Virology  Journal

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, with Kds 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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Autoantigens
  • Base Sequence
  • Cell Nucleus
  • Hepatitis B virus
  • Humans
  • Male
  • Mice
  • Mice, Transgenic
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Phosphorylation
  • RNA, Viral
  • RNA-Binding Proteins
  • Ribonucleoproteins
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Identity

PubMed Central ID

  • PMC112637

International Standard Serial Number (ISSN)

  • 0022-538X

PubMed ID

  • 10364328
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Additional Document Info

start page

  • 5767

end page

  • 5776

volume

  • 73

issue

  • 7

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