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Binding interaction of SARS coronavirus 3CL pro protease with vacuolar‐H + ATPase G1 subunit
Author(s) -
Lin Cheng-Wen,
Tsai Fuu-Jen,
Wan Lei,
Lai Chien-Chen,
Lin Kuan-Hsun,
Hsieh Tsung-Han,
Shiu Shi-Yi,
Li Jeng-Yi
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.075
Subject(s) - coronavirus , protein subunit , protease , covid-19 , virology , chemistry , microbiology and biotechnology , atpase , physics , biology , enzyme , biochemistry , medicine , gene , outbreak , disease , pathology , infectious disease (medical specialty)
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.