Structural basis of RNA polymerase complexes in African swine fever virus

Guoliang Zhu, Fei Xi, Wuxia Zeng, Yifei Zhao, Weijun Cao, Chen Liu, Fan Yang, Yi Ru, Shuqi Xiao, Shilei Zhang, Huanan Liu, Hong Tian, Fayu Yang, Biao Lu, Shukai Sun, Haiyang Song, Bozhang Sun, Xiaoyi Zhao, Lijie Tang, Kangli Li, Jijun He, Jianhong Guo, Yun Zhu (), Zixiang Zhu (), Fei Sun () and Haixue Zheng ()
Additional contact information
Guoliang Zhu: Chinese Academy of Agricultural Sciences
Fei Xi: Chinese Academy of Agricultural Sciences
Wuxia Zeng: Chinese Academy of Agricultural Sciences
Yifei Zhao: Chinese Academy of Agricultural Sciences
Weijun Cao: Chinese Academy of Agricultural Sciences
Chen Liu: Chinese Academy of Agricultural Sciences
Fan Yang: Chinese Academy of Agricultural Sciences
Yi Ru: Chinese Academy of Agricultural Sciences
Shuqi Xiao: Chinese Academy of Agricultural Sciences
Shilei Zhang: Chinese Academy of Agricultural Sciences
Huanan Liu: Chinese Academy of Agricultural Sciences
Hong Tian: Chinese Academy of Agricultural Sciences
Fayu Yang: Chinese Academy of Agricultural Sciences
Biao Lu: Chinese Academy of Agricultural Sciences
Shukai Sun: Chinese Academy of Agricultural Sciences
Haiyang Song: Chinese Academy of Agricultural Sciences
Bozhang Sun: Chinese Academy of Agricultural Sciences
Xiaoyi Zhao: Chinese Academy of Agricultural Sciences
Lijie Tang: Northeast Agricultural University
Kangli Li: Chinese Academy of Agricultural Sciences
Jijun He: Chinese Academy of Agricultural Sciences
Jianhong Guo: Chinese Academy of Agricultural Sciences
Yun Zhu: Chinese Academy of Sciences
Zixiang Zhu: Chinese Academy of Agricultural Sciences
Fei Sun: Chinese Academy of Sciences
Haixue Zheng: Chinese Academy of Agricultural Sciences

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract African swine fever virus is highly contagious and causes a fatal infectious disease in pigs, resulting in a significant global impact on pork supply. The African swine fever virus RNA polymerase serves as a crucial multifunctional protein complex responsible for genome transcription and regulation. Therefore, it is essential to investigate its structural and functional characteristics for the prevention and control of African swine fever. Here, we determine the structures of endogenous African swine fever virus RNA polymerase in both nucleic acid-free and elongation states. The African swine fever virus RNA polymerase shares similarities with the core of typical RNA polymerases, but possesses a distinct subunit M1249L. Notably, the dynamic binding mode of M1249L with RNA polymerase, along with the C-terminal tail insertion of M1249L in the active center of DNA-RNA scaffold binding, suggests the potential of M1249L to regulate RNA polymerase activity within cells. These results are important for understanding the transcription cycle of the African swine fever virus and for developing antiviral strategies.

Date: 2025
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DOI: 10.1038/s41467-024-55683-z

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