Coronavirus infectious bronchitis virus non-structural proteins 8 and 12 form stable complex independent of the non-translated regions of viral RNA and other viral proteins

Virology. 2018 Jan 1:513:75-84. doi: 10.1016/j.virol.2017.10.004. Epub 2017 Oct 13.

Abstract

The cleavage products from coronavirus polyproteins, known as the non-structural proteins (nsps), are believed to make up the major components of the viral replication/transcription complex. In this study, several nsps encoded by avian gammacoronavirus infectious bronchitis virus (IBV) were screened for RNA-binding activity and interaction with its RNA-dependent RNA polymerase, nsp12. Nsp2, nsp5, nsp8, nsp9 and nsp10 were found to bind to untranslated regions (UTRs), while nsp8 was confirmed to interact with nsp12. Nsp8 has been reported to interact with nsp7 and functions as a primase synthesizing RNA primers for nsp12. Further characterization revealed that nsp8-nsp12 interaction is independent of the UTRs of viral RNA, and nsp8 interacts with both the N- and C-terminal regions of nsp12. These results have prompted a proposal of how the nsp7-nsp8 complex could possibly function in tandem with nsp12, forming a highly efficient complex that could synthesize both the RNA primer and viral RNA during coronavirus infection.

Keywords: Coronavirus; IBV; Infectious bronchitis virus; Non-structure protein; Protein interaction; RNA synthesis; RNA-dependent RNA polymerase; Viral genome replication.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Humans
  • Infectious bronchitis virus / physiology*
  • Protein Binding
  • Protein Multimerization*
  • RNA, Viral / metabolism
  • RNA-Binding Proteins / metabolism*
  • Viral Nonstructural Proteins / metabolism*

Substances

  • RNA, Viral
  • RNA-Binding Proteins
  • Viral Nonstructural Proteins