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ANP32B is a nuclear target of henipavirus M proteins.
Bauer, Anja; Neumann, Sebastian; Karger, Axel; Henning, Ann-Kristin; Maisner, Andrea; Lamp, Boris; Dietzel, Erik; Kwasnitschka, Linda; Balkema-Buschmann, Anne; Keil, Günther M; Finke, Stefan.
Affiliation
  • Bauer A; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
  • Neumann S; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
  • Karger A; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
  • Henning AK; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
  • Maisner A; Institute of Virology, Philipps-University Marburg, Marburg, Germany.
  • Lamp B; Institute of Virology, Philipps-University Marburg, Marburg, Germany.
  • Dietzel E; Institute of Virology, Philipps-University Marburg, Marburg, Germany.
  • Kwasnitschka L; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald - Insel Riems, Germany.
  • Balkema-Buschmann A; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald - Insel Riems, Germany.
  • Keil GM; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
  • Finke S; Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
PLoS One ; 9(5): e97233, 2014.
Article in En | MEDLINE | ID: mdl-24823948
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Nuclear Proteins / Cell Nucleus / Viral Matrix Proteins / Hendra Virus / Multiprotein Complexes Limits: Humans Language: En Journal: PLoS One Year: 2014 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Nuclear Proteins / Cell Nucleus / Viral Matrix Proteins / Hendra Virus / Multiprotein Complexes Limits: Humans Language: En Journal: PLoS One Year: 2014 Document type: Article