Document Detail


Binding interaction of SARS coronavirus 3CL(pro) protease with vacuolar-H+ ATPase G1 subunit.
MedLine Citation:
PMID:  16226257     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Cheng-Wen Lin; Fuu-Jen Tsai; Lei Wan; Chien-Chen Lai; Kuan-Hsun Lin; Tsung-Han Hsieh; Shi-Yi Shiu; Jeng-Yi Li
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-10-06
Journal Detail:
Title:  FEBS letters     Volume:  579     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2005 Nov 
Date Detail:
Created Date:  2005-11-04     Completed Date:  2005-12-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  6089-94     Citation Subset:  IM    
Affiliation:
Department of Medical Laboratory Science and Biotechnology, China Medical University, No. 91, Hsueh-Shih Road, Taichung 404, Taiwan. cwlin@mail.cmu.edu.tw
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Benzopyrans / metabolism
Cysteine Endopeptidases
Endopeptidases / genetics,  metabolism*
Humans
Hydrogen-Ion Concentration
Immunoprecipitation
Lung / enzymology*
Molecular Sequence Data
Naphthols / metabolism
Peptide Library
Protein Subunits / genetics,  metabolism
Recombinant Proteins / genetics,  metabolism
Rhodamines / metabolism
Vacuolar Proton-Translocating ATPases / genetics,  metabolism*
Viral Proteins / genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Benzopyrans; 0/Naphthols; 0/Peptide Library; 0/Protein Subunits; 0/Recombinant Proteins; 0/Rhodamines; 0/Viral Proteins; 0/seminaphthorhodaminefluoride; EC 3.4.-/Endopeptidases; EC 3.4.22.-/3C-like protease, SARS coronavirus; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.6.1.-/Vacuolar Proton-Translocating ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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