期刊
VIROLOGY
卷 346, 期 2, 页码 251-257出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2006.01.007
关键词
Nipah; fusion protein; cathepsin L; proteolytic processing
类别
资金
- NIAID NIH HHS [AI063052, R21 AI063052, R01 AI051517] Funding Source: Medline
The Nipah virus fusion (F) protein is proteolytically processed to F-1 + F-2 subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B Could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form. (C) 2006 Elsevier Inc. All rights reserved.
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