Structural Basis of RNA Polymerase Complexes in African Swine Fever Virus

Overview

Journal Nat Commun

Date 2025 Jan 8

PMID 39779680

Authors

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

Haixue Zheng

Affiliations

Soon will be listed here.

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.

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