A Single Mutation at Position 120 in the Envelope Protein Attenuates Tembusu Virus in Ducks
文献类型: 外文期刊
作者: Yan, Dawei 1 ; Wang, Binbin 1 ; Shi, Ying 1 ; Ni, Xintao 1 ; Wu, Xiaogang 1 ; Li, Xuesong 1 ; Liu, Xingpo 1 ; Wang, Haiwang 1 ; Su, Xin 1 ; Teng, Qiaoyang 1 ; Yang, Jianmei 1 ; Liu, Qinfang 1 ; Li, Zejun 1 ;
作者机构: 1.Chinese Acad Agr Sci, Shanghai Vet Res Inst, Dept Avian Infect Dis, Shanghai 200241, Peoples R China
2.Shanghai Acad Agr Sci, Inst Anim Husb & Vet Sci, Shanghai 201106, Peoples R China
关键词: Tembusu virus; envelope protein; attenuation; tissue tropism; transmissibility
期刊名称:VIRUSES-BASEL ( 影响因子:5.818; 五年影响因子:5.811 )
ISSN:
年卷期: 2022 年 14 卷 3 期
页码:
收录情况: SCI
摘要: A live attenuated duck Tembusu virus (TMUV) vaccine FX2010-180P (180P) was successfully utilized to prevent TMUV infections in ducks in China. Compared with wild-type TMUV, 180P was highly attenuated and lost transmissibility in ducks. However, the mechanism of the attenuation of 180P remains poorly understood. To explore the key molecular basis of attenuation, chimeric and site mutant viruses in the background of the wild-type TMUV-FX2010 (FX) strain were rescued, and the replication, tissue tropism, and transmissibility were characterized in ducks. The results show that the envelope (E) protein was responsible for attenuation and loss of transmission in ducks. Further studies showed that a D120N amino acid mutation located in domain II of the E protein was responsible for the attenuation and transmissibility loss of 180P in ducks. The D120N substitution resulted in an extra high-mannose type N-linked glycosylation (NLG) in the E protein of 180P compared with the wild-type TMUV, which might restrict the tissue tropism and transmissibility of TMUV in ducks. Our findings elucidate that N120 in the E protein is a key molecular basis of TMUV attenuation in ducks and provide new insight into the role of NLG in TMUV tissue tropism and transmissibility.
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