title: A single herpesvirus protein can mediate vesicle formation in the nuclear envelope.
abstract: Herpesviruses assemble capsids in the nucleus and egress by unconventional vesicle-mediated trafficking through the nuclear envelope. Capsids bud at the inner nuclear membrane into the nuclear envelope lumen. The resulting intralumenal vesicles fuse with the outer nuclear membrane, delivering the capsids to the cytoplasm. Two viral proteins are required for vesicle formation, the tail-anchored pUL34 and its soluble interactor, pUL31. Whether cellular proteins are involved is unclear. Using giant unilamellar vesicles, we show that pUL31 and pUL34 are sufficient for membrane budding and scission. pUL34 function can be bypassed by membrane tethering of pUL31, demonstrating that pUL34 is required for pUL31 membrane recruitment but not for membrane remodeling. pUL31 can inwardly deform membranes by oligomerizing on their inner surface to form buds that constrict to vesicles. Therefore, a single viral protein can mediate all events necessary for membrane budding and abscission.
authors.affiliation: From the Friedrich Miescher Laboratory of the Max Planck Society, 72076 Tübingen, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Lorenz
authors.affiliation: From the Friedrich Miescher Laboratory of the Max Planck Society, 72076 Tübingen, Germany.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Vollmer
authors.affiliation: the Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and.
authors.forename: Joseph D
authors.initials: JD
authors.lastname: Unsay
authors.affiliation: the Friedrich Loeffler Institute, Federal Research Institute for Animal Health, 17493 Greifswald, Germany.
authors.forename: Barbara G
authors.initials: BG
authors.lastname: Klupp
authors.affiliation: the Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and.
authors.forename: Ana J
authors.initials: AJ
authors.lastname: García-Sáez
authors.affiliation: the Friedrich Loeffler Institute, Federal Research Institute for Animal Health, 17493 Greifswald, Germany.
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Mettenleiter
authors.affiliation: From the Friedrich Miescher Laboratory of the Max Planck Society, 72076 Tübingen, Germany, wolfram.antonin@tuebingen.mpg.de.
authors.forename: Wolfram
authors.initials: W
authors.lastname: Antonin
mesh_terms: D000818:Animals; D001692:Biological Transport; D011558:Herpesvirus 1, Suid / Q000502:physiology*; D054884:Host-Pathogen Interactions; D008051:Lipid Bilayers / Q000378:metabolism; D008081:Liposomes / Q000378:metabolism; D009685:Nuclear Envelope / Q000378:metabolism / Q000821:virology*; D011557:Pseudorabies / Q000378:metabolism* / Q000821:virology*; D013552:Swine; D014764:Viral Proteins / Q000378:metabolism*; D057074:Virus Release
chemical_list: D008051:Lipid Bilayers; D008081:Liposomes; D014764:Viral Proteins
keywords: Herpesvirus; Membrane Reconstitution; Membrane Trafficking; Nuclear Envelope; Nuclear Translocation