title: Poxviruses Encode a Reticulon-Like Protein that Promotes Membrane Curvature.
abstract: Poxviruses are enveloped DNA viruses that replicate within the cytoplasm. The first viral structures are crescents and spherical particles, with a lipoprotein membrane bilayer, that are thought to be derived from the ER. We determined that A17, a conserved viral transmembrane protein essential for crescent formation, forms homo-oligomers and shares topological features with cellular reticulon-like proteins. The latter cell proteins promote membrane curvature and contribute to the tubular structure of the ER. When the purified A17 protein was incorporated into liposomes, 25 nm diameter vesicles and tubules formed at low and high A17 concentrations, respectively. In addition, intracellular expression of A17 in the absence of other viral structural proteins transformed the ER into aggregated three-dimensional (3D) tubular networks. We suggest that A17 is a viral reticulon-like protein that contributes to curvature during biogenesis of the poxvirus membrane.
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
authors.forename: Karl J
authors.initials: KJ
authors.lastname: Erlandson
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
authors.forename: Himani
authors.initials: H
authors.lastname: Bisht
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
authors.forename: Andrea S
authors.initials: AS
authors.lastname: Weisberg
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
authors.forename: Seong-In
authors.initials: SI
authors.lastname: Hyun
authors.affiliation: Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA.
authors.forename: Bryan T
authors.initials: BT
authors.lastname: Hansen
authors.affiliation: Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA.
authors.forename: Elizabeth R
authors.initials: ER
authors.lastname: Fischer
authors.affiliation: Structural Cell Biology Section, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA.
authors.forename: Jenny E
authors.initials: JE
authors.lastname: Hinshaw
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA. Electronic address: bmoss@nih.gov.
authors.forename: Bernard
authors.initials: B
authors.lastname: Moss
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D021961:Cell Membrane Structures / Q000648:ultrastructure* / Q000821:virology; D002522:Chlorocebus aethiops; D017124:Conserved Sequence; D004721:Endoplasmic Reticulum / Q000648:ultrastructure / Q000821:virology; D011212:Poxviridae / Q000235:genetics*; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology*
chemical_list: D014764:Viral Proteins