title: EBV early lytic protein BFRF1 alters emerin distribution and post-translational modification.
abstract: The nuclear envelope (NE), a structural element of fundamental importance for the cell, is the first barrier that meets a virus in the early stages of viral maturation. Therefore, in order to allow the passage of nucleocapsids, viruses are known to modulate the architecture of the nuclear membrane to permit a proficient viral infection. Epstein-Barr Virus (EBV), a pathogen from Herpesvirus family, possesses two well conserved proteins, BFRF1 and BFLF2, which together form the heterodimeric nuclear egress complex (NEC) that is involved in the early steps of nuclear egress. Here we show that EBV replication causes the delocalization of emerin, a cellular LEM-domain protein normally distributed on the nuclear rim. We also demonstrate that the early lytic protein BFRF1 is responsible for emerin delocalization. Expression of BFRF1 alone or in combination with BFLF2 induces emerin hyperphosphorylation. Altogether, these results suggest a novel mechanism by which EBV exploits the cellular machinery for nucleocapsid egress.
authors.affiliation: Dep. Experimental Medicine University of Rome "La Sapienza", Italy.
authors.forename: S
authors.initials: S
authors.lastname: Yadav
authors.affiliation: Dep. Experimental Medicine University of Rome "La Sapienza", Italy.
authors.forename: F
authors.initials: F
authors.lastname: Libotte
authors.affiliation: Dep. Experimental Medicine University of Rome "La Sapienza", Italy.
authors.forename: E
authors.initials: E
authors.lastname: Buono
authors.affiliation: Dep. Molecular Medicine University of Rome "La Sapienza", Italy.
authors.forename: S
authors.initials: S
authors.lastname: Valia
authors.affiliation: Boston University School of Medicine, Boston, MA, USA.
authors.forename: G A
authors.initials: GA
authors.lastname: Farina
authors.affiliation: Dep. Experimental Medicine University of Rome "La Sapienza", Italy.
authors.forename: A
authors.initials: A
authors.lastname: Faggioni
authors.affiliation: Dep. Experimental Medicine University of Rome "La Sapienza", Italy; Boston University School of Medicine, Boston, MA, USA. Electronic address: antonella.farina@uniroma1.it.
authors.forename: A
authors.initials: A
authors.lastname: Farina
mesh_terms: D021581:Active Transport, Cell Nucleus; D000818:Animals; D001402:B-Lymphocytes / Q000378:metabolism / Q000821:virology*; D002144:Callithrix; D045744:Cell Line, Tumor; D004854:Herpesvirus 4, Human / Q000235:genetics* / Q000378:metabolism; D054884:Host-Pathogen Interactions; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D009685:Nuclear Envelope / Q000378:metabolism / Q000821:virology; D009687:Nuclear Proteins / Q000235:genetics* / Q000378:metabolism; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism; D014771:Virion / Q000235:genetics / Q000378:metabolism; D019065:Virus Assembly; D057074:Virus Release; D014779:Virus Replication
chemical_list: C406064:BFRF1 protein, Human herpesvirus 4; D008565:Membrane Proteins; D009687:Nuclear Proteins; D014764:Viral Proteins; C092710:emerin
keywords: BFRF1; EBV; Emerin; Nuclear envelope; Viral egress