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Journal of Virology, July 1999, p. 5767-5776, Vol. 73, No. 7
Department of Molecular and Experimental
Medicine, The Scripps Research Institute, La Jolla, California
92037
Received 1 February 1999/Accepted 14 April 1999
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.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
La Autoantigen Specifically Recognizes a Predicted
Stem-Loop in Hepatitis B Virus RNA

*
Corresponding author. Mailing address: Department of
Molecular and Experimental Medicine, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (619) 784-8228. Fax: (619) 784-2160. E-mail: fchisari{at}scripps.edu.
Paper no. 11631-MEM from The Scripps Research Institute.
Present address: Heinrich-Pette-Institut für Experimentelle
Virologie und Immunologie, Universität Hamburg, D-20251 Hamburg, Germany.
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