ANP32B is a nuclear target of henipavirus M proteins.
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.
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Anja
A
Bauer
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Sebastian
S
Neumann
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Axel
A
Karger
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Ann-Kristin
AK
Henning
Institute of Virology, Philipps-University Marburg, Marburg, Germany.
Andrea
A
Maisner
Institute of Virology, Philipps-University Marburg, Marburg, Germany.
Boris
B
Lamp
Institute of Virology, Philipps-University Marburg, Marburg, Germany.
Erik
E
Dietzel
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald - Insel Riems, Germany.
Linda
L
Kwasnitschka
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald - Insel Riems, Germany.
Anne
A
Balkema-Buschmann
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Günther M
GM
Keil
Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Stefan
S
Finke
D002467:Cell Nucleus / Q000378:metabolism*; D019084:Fluorescent Antibody Technique, Indirect; D057809:HEK293 Cells; D045404:Hendra Virus / Q000378:metabolism*; D006801:Humans; D018613:Microscopy, Confocal; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D014162:Transfection; D014763:Viral Matrix Proteins / Q000378:metabolism*
C490341:ANP32B protein, human; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D014763:Viral Matrix Proteins