Mutagenesis of the di-leucine motif in the cytoplasmic tail of newcastle disease virus fusion protein modulates the viral fusion ability and pathogenesis

Virology Journal

Research

Yizhuo He¹  Ruihua Yang¹  Qingyuan Teng¹  Guozhong Zhang¹  Lihua Tang¹  Yahui Huang¹  Ye Zhao¹ 

[1] Key Laboratory of Animal Epidemiology of the Ministry of Agriculture, College of Veterinary Medicine, China Agricultural University, No. 2 Yuanmingyuan West Road, Haidian District, 100193, Beijing, China;

关键词: Newcastle disease virus;    Fusion protein;    Cytoplasmic tail;    Di-leucine motif;    Virus budding;   

DOI  :  10.1186/s12985-023-01985-5

 received in 2022-12-22, accepted in 2023-02-06,  发布年份 2023

来源: Springer

【 摘 要 】

BackgroundNewcastle disease virus (NDV) is a highly infectious viral disease, which can affect chickens and many other kinds of birds. The main virulence factor of NDV, the fusion (F) protein, is located on the viral envelope and plays a major role in the virus’ ability to penetrate cells and cause host cell fusion during infection. Multiple highly conserved tyrosine and di-leucine (LL) motifs in the cytoplasmic tail (CT) of the virus may contribute to F protein functionality in the viral life cycle.MethodsTo examine the contribution of the LL motif in the biosynthesis, transport, and function of the F protein, we constructed and rescued a NDV mutant strain, rSG10*-F/L537A, with an L537A mutation using a reverse genetic system. Subsequently, we compared the differences in the syncytium formation ability, pathogenicity, and replication levels of wild-type rSG10* and the mutated strain.ResultsCompared with rSG10*, rSG10*-F/L537A had attenuated syncytial formation and pathogenicity, caused by a viral budding defect. Further studies showed that the LL-motif mutation did not affect the replication, transcription, or translation of the virus genome but affected the expression of the F protein at the cell surface.ConclusionsWe concluded that the LL motif in the NDV F CT affected the regulation of F protein expression at the cell surface, thus modulating the viral fusion ability and pathogenic phenotype.

【 授权许可】

CC BY   
© The Author(s) 2023

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