A distinct class of plant and animal viral proteins that disrupt mitosis by directly interrupting the mitotic entry switch Wee1-Cdc25-Cdk1

Sci Adv. 2020 May 13;6(20):eaba3418. doi: 10.1126/sciadv.aba3418. eCollection 2020 May.

Abstract

Many animal viral proteins, e.g., Vpr of HIV-1, disrupt host mitosis by directly interrupting the mitotic entry switch Wee1-Cdc25-Cdk1. However, it is unknown whether plant viruses may use this mechanism in their pathogenesis. Here, we report that the 17K protein, encoded by barley yellow dwarf viruses and related poleroviruses, delays G2/M transition and disrupts mitosis in both host (barley) and nonhost (fission yeast, Arabidopsis thaliana, and tobacco) cells through interrupting the function of Wee1-Cdc25-CDKA/Cdc2 via direct protein-protein interactions and alteration of CDKA/Cdc2 phosphorylation. When ectopically expressed, 17K disrupts the mitosis of cultured human cells, and HIV-1 Vpr inhibits plant cell growth. Furthermore, 17K and Vpr share similar secondary structural feature and common amino acid residues required for interacting with plant CDKA. Thus, our work reveals a distinct class of mitosis regulators that are conserved between plant and animal viruses and play active roles in viral pathogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism
  • Mitosis
  • Nuclear Proteins / metabolism
  • Phosphoprotein Phosphatases / metabolism
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism
  • Schizosaccharomyces pombe Proteins* / metabolism
  • Schizosaccharomyces* / metabolism
  • Viral Proteins / metabolism

Substances

  • Cell Cycle Proteins
  • Nuclear Proteins
  • Schizosaccharomyces pombe Proteins
  • Viral Proteins
  • wee1 protein, S pombe
  • Protein-Tyrosine Kinases
  • Cdc25 protein, S pombe
  • Phosphoprotein Phosphatases