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Hepatitis B virus X protein interacts with β5 subunit of heterotrimeric guanine nucleotide binding protein
BACKGROUND: To isolate cellular proteins interacting with hepatitis B virus X protein (HBX), from HepG2 cells infected with hepatitis B virus (HBV). RESULTS: HBV particles were produced in culture medium of HepG2 cells transfected with the mammalian expression vector containing the linear HBV genome...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1215529/ https://www.ncbi.nlm.nih.gov/pubmed/16135253 http://dx.doi.org/10.1186/1743-422X-2-76 |
Sumario: | BACKGROUND: To isolate cellular proteins interacting with hepatitis B virus X protein (HBX), from HepG2 cells infected with hepatitis B virus (HBV). RESULTS: HBV particles were produced in culture medium of HepG2 cells transfected with the mammalian expression vector containing the linear HBV genome, as assessed by commercially available ELISA assay. A cDNA library was made from these cells exposed to HBV. From yeast two hybrid screening with HBX as bait, human guanine nucleotide binding protein β subunit 5L (GNβ5) was isolated from the cDNA library constructed in this study as a new HBX-interacting protein. The HBX-GNβ5 interaction was further supported by mammalian two hybrid assay. CONCLUSION: The use of a cDNA library constructed from HBV-transfected HepG2 cells has resulted in the isolation of new cellular proteins interacting with HBX. |
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