Structures of African swine fever virus topoisomerase complex and their implications

Jie Yang, Zhiwei Shao, Xin Zhao, Weizhen Zhang, Yixi Zhang, Linxi Li, Yanqing Gao, Qiyuan Shao, Chulei Cao, Huili Li, Ruixue Cui, Hehua Liu and Jianhua Gan ()
Additional contact information
Jie Yang: Fudan University
Zhiwei Shao: Fudan University
Xin Zhao: Fudan University
Weizhen Zhang: Fudan University
Yixi Zhang: Fudan University
Linxi Li: Fudan University
Yanqing Gao: Fudan University
Qiyuan Shao: Fudan University
Chulei Cao: Fudan University
Huili Li: Fudan University
Ruixue Cui: Shanghai Jiaotong University School of Medicine
Hehua Liu: Fudan University
Jianhua Gan: Fudan University

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: Abstract African swine fever virus (ASFV) is the causal agent of African swine fever (ASF), which is contagious and highly lethal to domestic pigs and wild boars. The genome of ASFV encodes many proteins important for ASFV life cycle. The functional importance of topoisomerase AsfvTopII has been confirmed by in vivo and in vitro assays, but the structure of AsfvTopII is poorly studied. Here, we report four AsfvTopII complex structures. The ATPase domain structures reveal the detailed basis for ATP binding and hydrolysis, which is shared by AsfvTopII and eukaryotic TopIIs. The DNA-bound structures show that AsfvTopII follows conserved mechanism in G-DNA binding and cleavage. Besides G-DNA, a T-DNA fragment is also captured in one AsfvTopII structure. Mutagenesis and in vitro assays confirm that Pro852 and the T-DNA-binding residue Tyr744 are important for the function of AsfvTopII. Our study not only advances the understanding on the biological function of AsfvTopII, but also provides a solid basis for the development of AsfvTopII-specific inhibitors.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-50981-y Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-50981-y

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-50981-y

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().