Two single mutations in the fusion protein of Newcastle disease virus confer hemagglutinin-neuraminidase independent fusion promotion and attenuate the pathogenicity in chickens

被引：19

作者：

Ji, Yanhong ^{[1
]}

Liu, Tao ^{[1
]}

Jia, Yane ^{[1
]}

Liu, Bin ^{[1
]}

Yu, Qingzhong ^{[2
]}

Cui, Xiaole ^{[1
]}

Guo, Fengfeng ^{[1
]}

Chang, Huiyun ^{[1
]}

Zhu, Qiyun ^{[1
]}

机构：

[1] Chinese Acad Agr Sci, Lanzhou Vet Res Inst, State Key Lab Vet Etiol Biol, Lanzhou 730046, Gansu, Peoples R China

[2] ARS, USDA, US Natl Poultry Res Ctr, Southeast Poultry Res Lab, Athens, GA 30605 USA

来源：

VIROLOGY | 2017年 / 509卷

基金：

中国国家自然科学基金;

关键词：

Newcastle disease virus; Fusion protein; Mutation; Independent fusion; Pathogenicity; AMINO-ACID SUBSTITUTIONS; HN PROTEIN; STRUCTURAL BASIS; MEMBRANE-FUSION; F-PROTEIN; GLYCOPROTEIN; REPLICATION; VIRULENCE; STALK;

D O I：

10.1016/j.virol.2017.06.021

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The fusion (F) protein of Newcastle disease virus (NDV) affects viral infection and pathogenicity through mediating membrane fusion. Previously, we found NDV with increased fusogenic activity in which contained T458D or G459D mutation in the F protein. Here, we investigated the effects of these two mutations on viral infection, fusogenicity and pathogenicity. Syncytium formation assays indicated that T458D or G459D increased the F protein cleavage activity and enhanced cell fusion with or without the presence of HN protein. The T458D- or G459D-mutated NDV resulted in a decrease in virus replication or release from cells. The animal study showed that the pathogenicity of the mutated NDVs was attenuated in chickens. These results indicate that these two single mutations in F altered or diminished the requirement of HN for promoting membrane fusion. The increased fusogenic activity may disrupt the cellular machinery and consequently decrease the virus replication and pathogenicity in chickens.

引用

页码：146 / 151

页数：6

共 28 条

[1]

Alexander D. J., 1998, LAB MANUAL ISOLATION, V4, P156

[2] Structural basis for paramyxovirus-mediated membrane fusion [J].