ANP32B is a nuclear target of henipavirus M proteins

• Published in: PloS one 2014-05, Vol.9 (5), p.e97233-e97233
• Main Authors: 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
• Format: Article
• Language: English
• Subjects: Accumulation; Apoptosis; Biology and Life Sciences; Budding; Cell Nucleus - metabolism; Cell survival; Fluorescent Antibody Technique, Indirect; Gene expression; Gene regulation; HEK293 Cells; Hendra Virus - metabolism; Humans; Infectious diseases; Leucine; Ligands; Localization; M protein; Matrix protein; Medicine and Health Sciences; Microscopy, Confocal; Molecular biology; Molecular modelling; Multiprotein Complexes - genetics; Multiprotein Complexes - metabolism; Nipah virus; Nuclear Proteins - metabolism; Nuclei; Overexpression; Protein transport; Proteins; Rabies; Replication; Respiratory syncytial virus; Rhabdoviridae; Ribonucleic acid; RNA; RNA viruses; Transfection; Viral Matrix Proteins - metabolism; Virology; Viruses
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0097233

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.