Nipah virus fusion protein: Influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin

被引：10

作者：

Diederich, Sandra ^{[1
]}

Dietzel, Erik ^{[1
]}

Maisner, Andrea ^{[1
]}

机构：

[1] Inst Virol, D-35043 Marburg, Germany

来源：

VIRUS RESEARCH | 2009年 / 145卷 / 02期

关键词：

Nipah virus; Fusion protein; Cleavage; Cathepsin L; Furin; Trypsin; SENDAI-VIRUS; HENDRA VIRUS; N-GLYCANS; PROTEOLYTIC CLEAVAGE; MAJOR DETERMINANT; EBOLA-VIRUS; AMINO-ACID; F-PROTEIN; ACTIVATION; GLYCOPROTEIN;

D O I：

10.1016/j.virusres.2009.07.020

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：300 / 306

页数：7