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Interaction of host cellular factor ANP32B with matrix proteins of different paramyxoviruses

Maria Günther1, Anja Bauer1, Martin Müller1

  • 1Institute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany.

The Journal of General Virology
|December 4, 2019
PubMed

Insights

Matrix (M) proteins from paramyxoviruses can interact with ANP32B, a host factor. This interaction is crucial for nuclear accumulation of some viral proteins, suggesting a conserved mechanism for host manipulation and immune regulation in infected hosts.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Non-segmented negative-strand RNA viruses (NNSVs) replicate in the cytoplasm, but their proteins often function in the nucleus.
  • Matrix (M) proteins of henipaviruses and other paramyxoviruses exhibit nuclear shuttling, interacting with host factors for modification and cell manipulation.
  • Acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) is known to interact with Hendra and Nipah virus M proteins, mediating their nuclear accumulation.

Purpose of the Study:

  • To investigate the interaction between paramyxovirus M proteins and ANP32B.
  • To determine the specific regions of ANP32 proteins involved in M protein binding.
  • To explore the role of ANP32B in the nuclear accumulation of various paramyxovirus M proteins.

Main Methods:

  • Co-immunoprecipitation and purification of M-ANP32 complexes.
  • Analysis of M protein binding to ANP32B with and without its nuclear localization signal (NLS).
  • Expression of various paramyxovirus M proteins and ANP32B in host cells.
  • Assessment of nuclear accumulation of M proteins under conditions of ANP32B overexpression and nuclear protein export inhibition.

Main Results:

  • The nuclear localization signal (NLS) of ANP32B is not essential for Hendra virus (HeV) M binding.
  • Neither the acidic nor the leucine-rich regions of ANP32 proteins directly mediate interaction with henipavirus M proteins.
  • Newcastle disease virus (NDV), Sendai virus (SeV), Measles virus (MeV), and Canine distemper virus (CDV) M proteins interact with ANP32B, unlike pneumovirus M.
  • NDV and SeV M proteins accumulate in the nucleus in an ANP32B-dependent manner, while morbillivirus M proteins do not, despite interaction.
  • The lack of nuclear accumulation for morbillivirus M proteins is attributed to intracellular compartmentalization preventing interaction with nuclear ANP32B.

Conclusions:

  • Paramyxovirus M proteins generally possess the ability to interact with ANP32B.
  • The interaction between M proteins and ANP32B suggests a conserved mechanism involved in host manipulation and immune regulation across paramyxoviruses.
  • Specific viral or host factors likely dictate the outcome of M-ANP32B interaction, such as nuclear accumulation.
Keywords:
ANP32Bhenipavirusmatrix proteinparamyxovirus matrix proteinsvirus-host interaction

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