TFIIH Transcription Factor, a Target for the Rift Valley Hemorrhagic Fever Virus

The Rift Valley fever virus (RVFV) is the causative agent of fatal hemorrhagic fever in humans and acute hepatitis in ruminants. We found that infection by RVFV leads to a rapid and drastic suppression of host cellular RNA synthesis that parallels a decrease of the TFIIH transcription factor cellula...

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Bibliographic Details
Published in:Cell 2004-02, Vol.116 (4), p.541-550
Main Authors: Le May, Nicolas, Dubaele, Sandy, De Santis, Luca Proietti, Billecocq, Agnès, Bouloy, Michèle, Egly, Jean-Marc
Format: Article
Language:English
Subjects:
Animals
Biochemistry, Molecular Biology
Cell Nucleus - metabolism
Cell Nucleus - virology
DNA, Complementary - metabolism
Gene Library
HeLa Cells
Humans
Life Sciences
Luciferases - metabolism
Mice
Microbiology and Parasitology
Microscopy, Confocal
Microscopy, Fluorescence
Molecular biology
Plasmids - metabolism
Protein Binding
Rift Valley fever virus
Rift Valley fever virus - metabolism
RNA - metabolism
TFIIH protein
Time Factors
Transcription Factor TFIIH
Transcription Factors, TFII - chemistry
Transcription Factors, TFII - metabolism
Transcription, Genetic
Two-Hybrid System Techniques
Virology
XPD protein
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Summary:The Rift Valley fever virus (RVFV) is the causative agent of fatal hemorrhagic fever in humans and acute hepatitis in ruminants. We found that infection by RVFV leads to a rapid and drastic suppression of host cellular RNA synthesis that parallels a decrease of the TFIIH transcription factor cellular concentration. Using yeast two hybrid system, recombinant technology, and confocal microscopy, we further demonstrated that the nonstructural viral NSs protein interacts with the p44 component of TFIIH to form nuclear filamentous structures that also contain XPB subunit of TFIIH. By competing with XPD, the natural partner of p44 within TFIIH, and sequestering p44 and XPB subunits, NSs prevents the assembly of TFIIH subunits, thus destabilizing the normal host cell life. These observations shed light on the mechanism utilized by RVFV to evade the host response.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(04)00132-1