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ANP32B is a nuclear target of henipavirus M proteins

Anja Bauer1, Sebastian Neumann1, Axel Karger1

  • 1Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.

Plos One
|May 15, 2014
PubMed

Insights

Hendra and Nipah virus matrix proteins interact with ANP32B, a nuclear protein. This interaction causes viral protein accumulation in the nucleus, potentially aiding virus replication and host cell manipulation.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Viral matrix (M) proteins drive membrane budding in negative-strand RNA viruses (NSVs) and manipulate host cells.
  • Cellular targets and mechanisms for many M proteins, including Nipah Virus (NiV) M, are poorly understood.
  • Nuclear trafficking of NiV M is crucial for virus release, but its nuclear targets remain unidentified.

Purpose of the Study:

  • To identify cellular interactors of henipavirus M proteins.
  • To elucidate the molecular mechanisms underlying M protein nuclear localization and function.

Main Methods:

  • Expression of tagged Hendra Virus (HeV) M proteins.
  • Isolation and analysis of M-containing protein complexes.
  • Over-expression studies of ANP32B and its effect on M protein localization.
  • Analysis in NiV-infected cells.

Main Results:

  • Acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) was identified as a potential interactor of HeV M protein.
  • Over-expression of ANP32B caused specific nuclear accumulation of HeV M.
  • ANP32B-dependent nuclear accumulation of M proteins was observed for both HeV and NiV, and in NiV-infected cells.
  • This suggests ANP32B interacts with henipavirus M during virus replication.

Conclusions:

  • ANP32B is a nuclear target of henipavirus M proteins.
  • ANP32B may contribute to virus replication by influencing M protein nuclear localization.
  • Potential implications for host cell survival and gene expression regulation are discussed.

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