期刊
VIROLOGY
卷 413, 期 2, 页码 265-274出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2011.02.020
关键词
SARS coronavirus; Spike protein; Proteolytic cleavage; Cathepsin L; Furin
类别
资金
- National Institute of Allergy And Infectious Diseases [R01AI074986, R21 AI059172, U54 AI57168, SFB 466/SFB 587, Graduiertenkolleg 1071]
- Center for Infection Biology at Hannover Medical School
- BMBF [01KI 0703]
Severe acute respiratory syndrome coronavirus (SARS-CoV) poses a considerable threat to human health. Activation of the viral spike (S)-protein by host cell proteases is essential for viral infectivity. However, the cleavage sites in SARS-S and the protease(s) activating SARS-S are incompletely defined. We found that R667 was dispensable for SARS-S-driven virus-cell fusion and for SARS-S-activation by trypsin and cathepsin Lin a virus-virus fusion assay. Mutation T760R, which optimizes the minimal furin consensus motif 758-RXXR-762, and furin overexpression augmented SARS-S activity, but did not result in detectable SARS-S cleavage. Finally. SARS-S-driven cell-cell fusion was independent of cathepsin L. a protease essential for virus-cell fusion. Instead, a so far unknown leupeptin-sensitive host cell protease activated cellular SARS-S for fusion with target cells expressing high levels of ACE2. Thus, different host cell proteases activate SARS-S for virus-cell and cell-cell fusion and SARS-S cleavage at R667 and 758-RXXR-762 can be dispensable for SARS-S activation. (C) 2011 Elsevier Inc. All rights reserved.
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