ANP32B is a nuclear target of henipavirus M proteins

PLoS One. 2014 May 13;9(5):e97233. doi: 10.1371/journal.pone.0097233. eCollection 2014.

Abstract

Membrane envelopment and budding of negative strand RNA viruses (NSVs) is mainly driven by viral matrix proteins (M). In addition, several M proteins are also known to be involved in host cell manipulation. Knowledge about the cellular targets and detailed molecular mechanisms, however, is poor for many M proteins. For instance, Nipah Virus (NiV) M protein trafficking through the nucleus is essential for virus release, but nuclear targets of NiV M remain unknown. To identify cellular interactors of henipavirus M proteins, tagged Hendra Virus (HeV) M proteins were expressed and M-containing protein complexes were isolated and analysed. Presence of acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) in the complex suggested that this protein represents a direct or indirect interactor of the viral matrix protein. Over-expression of ANP32B led to specific nuclear accumulation of HeV M, providing a functional link between ANP32B and M protein. ANP32B-dependent nuclear accumulation was observed after plasmid-driven expression of HeV and NiV matrix proteins and also in NiV infected cells. The latter indicated that an interaction of henipavirus M protein with ANP32B also occurs in the context of virus replication. From these data we conclude that ANP32B is a nuclear target of henipavirus M that may contribute to virus replication. Potential effects of ANP32B on HeV nuclear shuttling and host cell manipulation by HeV M affecting ANP32B functions in host cell survival and gene expression regulation are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Nucleus / metabolism*
  • Fluorescent Antibody Technique, Indirect
  • HEK293 Cells
  • Hendra Virus / metabolism*
  • Humans
  • Microscopy, Confocal
  • Multiprotein Complexes / genetics
  • Multiprotein Complexes / metabolism*
  • Nuclear Proteins / metabolism*
  • Transfection
  • Viral Matrix Proteins / metabolism*

Substances

  • ANP32B protein, human
  • Multiprotein Complexes
  • Nuclear Proteins
  • Viral Matrix Proteins

Grants and funding

This study was supported by institutional funding of the Friedrich-Loeffler-Institut (www.fli.bund.de) and by the Deutsche Forschungsgemeinschaft through grant DFG FI941/3-1 (www.dfg.de). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.