title: Assembly of monomeric human cytomegalovirus pUL104 into portal structures.
abstract: In order for human cytomegalovirus (HCMV) to replicate, concatemeric DNA has to be cleaved into unit-length genomes and packaged into preformed capsids. For packaging to take place and DNA to be translocated, a channel is required in the capsid. Viral capsid channels are generally formed by portal proteins. Here, we show by cross-linking, native gel electrophoresis of infected cells and gel permeation chromatography that the HCMV portal candidate protein pUL104 can form dimers and higher order multimers. Electron microscopy of purified monomeric pUL104 after 5 min incubation revealed that the protein had assembled into a multimeric form and that this form closely resembles complete portal assembly. This is the first study to show that pUL104 monomers have the ability to form portal complexes without additional viral proteins.
authors: Microscopy and Imaging Center, Department of Biology and Department of Biochemistry and Biophysics, Texas A & M University, College Station, TX 77843-2257, USA.
authors: Andreas
authors: A
authors: Holzenburg
authors: Institute of Virology, Helmut-Ruska Haus, Charité Campus Mitte, University Medicine Berlin, Berlin, Germany.
authors: Alexandra
authors: A
authors: Dittmer
authors: Institute of Virology, Helmut-Ruska Haus, Charité Campus Mitte, University Medicine Berlin, Berlin, Germany.
authors: Elke
authors: E
authors: Bogner
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D002850:Chromatography, Gel; D003587:Cytomegalovirus / Q000145:classification / Q000235:genetics* / Q000502:physiology*; D015180:Electrophoresis, Gel, Two-Dimensional; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D006801:Humans; D007313:Insecta / Q000166:cytology; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D019065:Virus Assembly / Q000502:physiology*
chemical_list: D014764:Viral Proteins