The MERS-CoV N Protein Regulates Host Cytokinesis and Protein Translation via Interaction With EF1A

Middle East respiratory syndrome coronavirus (MERS-CoV), a pathogen causing severe respiratory disease in humans that emerged in June 2012, is a novel beta coronavirus similar to severe acute respiratory syndrome coronavirus (SARS-CoV). In this study, immunoprecipitation and proximity ligation assay...

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Veröffentlicht in:Frontiers in microbiology 2021-06, Vol.12, p.551602-551602
Hauptverfasser: Zhu, Lin, Gao, Ting, Fu, Yangbo, Han, Xiujing, Yue, Junjie, Liu, Yaoning, Liu, Hainan, Dong, Qincai, Yang, Weihong, Hu, Yong, Jin, Yanwen, Li, Ping, Liu, Xuan, Cao, Cheng
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Sprache:eng
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Zusammenfassung:Middle East respiratory syndrome coronavirus (MERS-CoV), a pathogen causing severe respiratory disease in humans that emerged in June 2012, is a novel beta coronavirus similar to severe acute respiratory syndrome coronavirus (SARS-CoV). In this study, immunoprecipitation and proximity ligation assays revealed that the nucleocapsid (N) protein of MERS-CoV interacted with human translation elongation factor 1A (EF1A), an essential component of the translation system with important roles in protein translation, cytokinesis, and filamentous actin (F-actin) bundling. The C-terminal motif (residues 359–363) of the N protein was the crucial domain involved in this interaction. The interaction between the MERS-CoV N protein and EF1A resulted in cytokinesis inhibition due to the formation of inactive F-actin bundles, as observed in an in vitro actin polymerization assay and in MERS-CoV-infected cells. Furthermore, the translation of a CoV-like reporter mRNA carrying the MERS-CoV 5′UTR was significantly potentiated by the N protein, indicating that a similar process may contribute to EF1A-associated viral protein translation. This study highlights the crucial role of EF1A in MERS-CoV infection and provides new insights into the pathogenesis of coronavirus infections.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2021.551602