title: Electron cryotomography reveals the portal in the herpesvirus capsid.
abstract: Herpes simplex virus type 1 is a human pathogen responsible for a range of illnesses from cold sores to encephalitis. The icosahedral capsid has a portal at one fivefold vertex which, by analogy to portal-containing phages, is believed to mediate genome entry and exit. We used electron cryotomography to determine the structure of capsids lacking pentons. The portal vertex appears different from pentons, being located partially inside the capsid shell, a position equivalent to that of bacteriophage portals. Such similarity in portal organization supports the idea of the evolutionary relatedness of these viruses.
authors.affiliation: Graduate Program in Structural and Computational Biology and Molecular Biophysics, National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
authors.forename: Juan T
authors.initials: JT
authors.lastname: Chang
authors.forename: Michael F
authors.initials: MF
authors.lastname: Schmid
authors.forename: Frazer J
authors.initials: FJ
authors.lastname: Rixon
authors.forename: Wah
authors.initials: W
authors.lastname: Chiu
mesh_terms: D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins / Q000302:isolation & purification; D020285:Cryoelectron Microscopy; D004591:Electrophoresis, Polyacrylamide Gel; D018259:Herpesvirus 1, Human / Q000737:chemistry*; D008958:Models, Molecular; D014054:Tomography; D014508:Urea
chemical_list: D036022:Capsid Proteins; D014508:Urea