Critical role for voltage-dependent anion channel 2 in infectious bursal disease virus-induced apoptosis in host cells via interaction with VP5

J Virol. 2012 Feb;86(3):1328-38. doi: 10.1128/JVI.06104-11. Epub 2011 Nov 23.

Abstract

Infectious bursal disease (IBD) is an acute, highly contagious, and immunosuppressive avian disease caused by IBD virus (IBDV). Although IBDV-induced host cell apoptosis has been established, the underlying molecular mechanism is still unclear. We report here that IBDV viral protein 5 (VP5) is a major apoptosis inducer in DF-1 cells by interacting with the voltage-dependent anion channel 2 (VDAC2) in the mitochondrion. We found that in DF-1 cells, VP5-induced apoptosis can be completely abolished by 4,4'-diisothiocyanatostibene-2,2'-disulfonic acid (DIDS), an inhibitor of VDAC. Furthermore, knockdown of VDAC2 by small interfering RNA markedly inhibits IBDV-induced apoptosis associated with decreased caspase-9 and -3 activation and cytochrome c release, leading to increased IBDV growth in host cells. Thus, VP5-induced apoptosis during IBDV infection is mediated by interacting with VDAC2, a protein that appears to restrict viral replication via induction of cell death.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / physiology*
  • Base Sequence
  • Cell Line
  • DNA Primers
  • Gene Knockdown Techniques
  • Humans
  • Infectious bursal disease virus / physiology*
  • Molecular Sequence Data
  • Protein Binding
  • Viral Nonstructural Proteins / metabolism*
  • Virus Replication
  • Voltage-Dependent Anion Channel 2 / genetics
  • Voltage-Dependent Anion Channel 2 / metabolism
  • Voltage-Dependent Anion Channel 2 / physiology*

Substances

  • DNA Primers
  • VP5 protein, infectious bursal disease virus
  • Viral Nonstructural Proteins
  • Voltage-Dependent Anion Channel 2