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J. Biol. Chem., Vol. 277, Issue 38, 34949-34958, September 20, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/38/34949    most recent M201911200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Horke, S. Articles by Heise, T. Search for Related Content PubMed PubMed Citation Articles by Horke, S. Articles by Heise, T. Social Bookmarking                      What's this?

Molecular Characterization of the Human La Protein·Hepatitis B Virus RNA.B Interaction in Vitro^*

Sven Horke, Kerstin Reumann, Andreas Rang, and Tilman Heise^§

From the Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie Universität Hamburg, Martinistrasse 52, Hamburg D-20251, Germany

The La protein was recently identified as a host factor potentially involved in the cytokine-induced post-transcriptional down-regulation of hepatitis B virus (HBV) RNA. The La binding site was mapped to a predicted stem-loop structure within a region shared by all HBV RNAs, and it was concluded that the La protein might be an HBV RNA-stabilizing factor. To characterize the RNA binding mediated by the different RNA recognition motifs (RRMs) of the human La protein, several La deletion mutants were produced and analyzed for HBV RNA binding ability. The data demonstrate that the first RRM is not required for binding, whereas the RNP-1 and RNP-2 consensus sequences of the RRM-2 and RRM-3 are separately required for binding, indicating a cooperative function of these two RRMs. Furthermore, the results suggest that multimeric La disassembles into monomeric La upon binding of HBV RNA.B. By gel retardation assay the affinity of the wild type human La·HBV RNA.B interaction was determined in the nanomolar range, comparable to the affinity determined for the mouse La·HBV RNA.B interaction. This study identified small regions within the human La protein mediating the binding of HBV RNA. Hence, these binding sites might represent targets for novel antiviral strategies based on the disruption of the human La·HBV RNA interaction, thereby leading to HBV RNA degradation.

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