Interaction between Translocation-associated membrane protein 1 and σC protein of novel duck reovirus controls virus infectivity

• Published in: Virus genes Vol. 56; no. 3; pp. 347 - 353
• Main Authors: Xiao, Rong, Mi, Xiaoyun, Sun, Jiahui, Ding, Mingyang, Li, Chuanfeng, Zhu, Jie, Liu, Guangqing, Ma, Wenge, Zhou, Hailong, Chen, Zongyan
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.06.2020; Springer Nature B.V
• Subjects: Biomedical and Life Sciences; Biomedicine; Capsid protein; Confocal microscopy; Genomes; Glutathione transferase; Immunoprecipitation; Infectivity; Mass spectroscopy; Medical Microbiology; Membrane proteins; Original Paper; Plant Sciences; Protein transport; Proteins; Replication; siRNA; Virology; Replication; TRAM1; siRNA; Protein interaction; σc protein; Novel duck reovirus
• ISSN: 0920-8569; 1572-994X
• DOI: 10.1007/s11262-020-01750-8

Novel duck reovirus (NDRV), the prototype strain of the species Avian orthoreovirus (ARV), is associated with high mortality in Pekin ducklings. σC is an outer capsid protein encoded by the S1 genome segment of NDRV which mediates attachment to host cells. Our previous studies using immunoprecipitation and mass spectrometry found that σC coprecipitated with some host proteins including Translocation-associated membrane protein 1 (TRAM1). However, the interaction between σC and TRAM1 has not been further confirmed experimentally. In this study, we utilized coimmunoprecipitation assays, glutathione S-transferase pull-down, and confocal microscopy to confirm the interaction between σC and TRAM1. In addition, knockdown of TRAM1 using siRNA and overexpression of TRAM1 gene were conducted to explore its effect on virus replication. The result showed that TRAM1 silencing benefits while overexpression inhibits viral replication. This study confirms the important role TRAM1 during NDRV infection which can help develop new approaches for NDRV disease prevention and control.