Binding interaction of SARS coronavirus 3CLproprotease with vacuolar-H+ATPase G1 subunit
| Autor: | Chien-Chen Lai, Cheng Wen Lin, Jeng Yi Li, Lei Wan, Shi Yi Shiu, Kuan Hsun Lin, Fuu Jen Tsai, Tsung Han Hsieh |
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| Rok vydání: | 2005 |
| Předmět: |
Vacuolar Proton-Translocating ATPases
Phage display Immunoprecipitation Protein subunit ATPase medicine.medical_treatment Molecular Sequence Data Biophysics Naphthols Cleavage (embryo) Biochemistry Article Viral Proteins Peptide Library Structural Biology Endopeptidases Human lung cDNA libraries Genetics medicine Humans Benzopyrans Amino Acid Sequence Lung Molecular Biology Coronavirus 3C Proteases Protease biology Rhodamines cDNA library Vacuolar-H+ ATPase G1 3CLpro Cell Biology Hydrogen-Ion Concentration Molecular biology Fusion protein Recombinant Proteins Cysteine Endopeptidases Protein Subunits SARS-coronavirus biology.protein |
| Zdroj: | Febs Letters |
| ISSN: | 0014-5793 |
| Popis: | The pathogenesis of severe acute respiratory syndrome coronavirus (SARS-CoV) is an important issue for treatment and prevention of SARS. Recently, SARS-CoV 3CL(pro) protease has been implied to be possible relevance to SARS-CoV pathogenesis. In this study, we intended to identify potential 3CL(pro)-interacting cellular protein(s) using the phage-displayed human lung cDNA library. The vacuolar-H+ ATPase (V-ATPase) G1 subunit that contained a 3CL(pro) cleavage site-like motif was identified as a 3CL(pro)-interacting protein, as confirmed using the co-immunoprecipitation assay and the relative affinity assay. In addition, our result also demonstrated the cleavage of the V-ATPase G1 fusion protein and the immunoprecipitation of cellular V-ATPase G1 by the 3CL(pro). Moreover, loading cells with SNARF-1 pH-sensitive dye showed that the intracellular pH in 3CL(pro)-expressing cells was significantly lower as compared to mock cells. |
| Databáze: | OpenAIRE |
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