کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3429737 | 1228255 | 2009 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Nipah virus fusion protein: Influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin Nipah virus fusion protein: Influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin](/preview/png/3429737.png)
Nipah virus (NiV), a highly pathogenic member of the Paramyxoviridae which originated from bats, encodes for a fusion (F) protein which is proteolytically processed within endosomes by cathepsin L. We show here that sequence requirements for NiV F activation differ markedly from other para- or orthomyxoviral fusion proteins. In contrast to other viral fusion proteins with monobasic cleavage sites, processing of NiV F proteins with one single basic amino acid in the cleavage peptide by exogenous trypsin is very inefficient, and introduction of a consensus sequence for furin does not result in cleavage by this ubiquitous protease. In contrast, a multibasic cleavage peptide in the NiV F protein completely impairs proteolytic processing and the generation of biological activity.
Journal: Virus Research - Volume 145, Issue 2, November 2009, Pages 300–306