Key result
Electron microscopy of the hepatitis C virus internal ribosome entry site revealed a distinct three-stemmed morphology that differs markedly from the picornavirus FMDV IRES.
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This study provides the first direct visualization of the HCV IRES tertiary structure, demonstrating a distinct three-stemmed architecture that binds PTB at domain III.
Translation of hepatitis C virus (HCV) RNA is initiated via the internal ribosome entry site (IRES), located within the 5' untranslated region. Although the secondary structure of this element has been predicted, little information on the tertiary structure is available. Here we report the first structural characterization of the HCV IRES using electron microscopy. In vitro transcribed RNA appeared as particles with characteristic morphology and gold labeling using a specific oligonucleotide confirmed them to be HCV IRES. Dimerization of the IRES by hybridization with tandem repeat oligonucleotides allowed the identification of domain III and an assignment of domains II and IV to distinct regions within the molecule. Using immunogold labeling, the pyrimidine tract binding protein (PTB) was shown to bind to domain III. Structure-function relationships based on the flexible hinge between domains II and III are suggested. Finally, the architecture of the HCV IRES was seen to be markedly different from that of a picornavirus, foot-and-mouth disease virus (FMDV).
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Beales et al. (2001) studied Hepatitis C virus. Electron microscopy and in vitro transcription vs. Foot-and-mouth disease virus (FMDV) IRES was evaluated on Structural characterization of the HCV internal ribosome entry site (IRES). Electron microscopy of the hepatitis C virus internal ribosome entry site revealed a distinct three-stemmed morphology that differs markedly from the picornavirus FMDV IRES.
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