Helicase of type 2 porcine reproductive and respiratory syndrome virus strain HV reveals a unique structure

Chenjun Tang, Zengqin Deng, Xiaorong Li, Meiting Yang, Zizi Tian, Zhenhang Chen, Guoguo Wang, Wei Wu, Wen hai Feng, Gongyi Zhang, Zhongzhou Chen

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Porcine reproductive and respiratory syndrome virus (PRRSV) is prevalent throughout the world and has caused great economic losses to the swine industry. Nonstructural protein 10 (nsp10) is a superfamily 1 helicase participating in multiple processes of virus replication and one of the three most conserved proteins in nidoviruses. Here we report three high resolution crystal structures of highly pathogenic PRRSV nsp10. PRRSV nsp10 has multiple domains, including an N-terminal zinc-binding domain (ZBD), a β-barrel domain, a helicase core with two RecA-like domains, and a C-terminal domain (CTD). The CTD adopts a novel fold and is required for the overall structure and enzymatic activities. Although each domain except the CTD aligns well with its homologs, PRRSV nsp10 adopts an unexpected extended overall structure in crystals and solution. Moreover, structural and functional analyses of PRRSV nsp10 versus its closest homolog, equine arteritis virus nsp10, suggest that DNA binding might induce a profound conformational change of PRRSV nsp10 to exert functions, thus shedding light on the mechanisms of activity regulation of this helicase.

Original languageEnglish
Article number215
JournalViruses
Volume12
Issue number2
DOIs
StatePublished - Jan 1 2020
Externally publishedYes

Keywords

  • Crystal structures
  • Helicase
  • Novel domain
  • Porcine reproductive and respiratory syndrome virus
  • SAXS
  • Zinc-binding domain

Fingerprint Dive into the research topics of 'Helicase of type 2 porcine reproductive and respiratory syndrome virus strain HV reveals a unique structure'. Together they form a unique fingerprint.

Cite this