title: A novel virus-host cell membrane interaction. Membrane voltage-dependent endocytic-like entry of bacteriophage straight phi6 nucleocapsid.
abstract: Studies on the virus-cell interactions have proven valuable in elucidating vital cellular processes. Interestingly, certain virus-host membrane interactions found in eukaryotic systems seem also to operate in prokaryotes (Bamford, D.H., M. Romantschuk, and P. J. Somerharju, 1987. EMBO (Eur. Mol. Biol. Organ.) J. 6:1467-1473; Romantschuk, M., V.M. Olkkonen, and D.H. Bamford. 1988. EMBO (Eur. Mol. Biol. Organ.) J. 7:1821-1829). straight phi6 is an enveloped double-stranded RNA virus infecting a gram-negative bacterium. The viral entry is initiated by fusion between the virus membrane and host outer membrane, followed by delivery of the viral nucleocapsid (RNA polymerase complex covered with a protein shell) into the host cytosol via an endocytic-like route. In this study, we analyze the interaction of the nucleocapsid with the host plasma membrane and demonstrate a novel approach for dissecting the early events of the nucleocapsid entry process. The initial binding of the nucleocapsid to the plasma membrane is independent of membrane voltage (DeltaPsi) and the K(+) and H(+) gradients. However, the following internalization is dependent on plasma membrane voltage (DeltaPsi), but does not require a high ATP level or K(+) and H(+) gradients. Moreover, the nucleocapsid shell protein, P8, is the viral component mediating the membrane-nucleocapsid interaction.
authors.affiliation: Institute of Biotechnology, FIN-00014, University of Helsinki, Helsinki, Finland.
authors.forename: M M
authors.initials: MM
authors.lastname: Poranen
authors.forename: R
authors.initials: R
authors.lastname: Daugelavicius
authors.forename: P M
authors.initials: PM
authors.lastname: Ojala
authors.forename: M W
authors.initials: MW
authors.lastname: Hess
authors.forename: D H
authors.initials: DH
authors.lastname: Bamford
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000327:Adsorption / Q000187:drug effects; D017126:Bacteriophage phi 6 / Q000187:drug effects / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D002462:Cell Membrane / Q000187:drug effects / Q000502:physiology* / Q000648:ultrastructure; D004579:Electron Transport / Q000187:drug effects; D004705:Endocytosis / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials / Q000187:drug effects; D008854:Microscopy, Electron; D009500:Neutralization Tests; D019251:Nucleocapsid / Q000187:drug effects / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D011188:Potassium / Q000037:antagonists & inhibitors / Q000378:metabolism; D054328:Proton Pump Inhibitors; D017494:Proton Pumps / Q000378:metabolism; D018892:Proton-Motive Force / Q000187:drug effects; D011549:Pseudomonas / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology*; D013104:Spheroplasts / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology; D013696:Temperature; D013997:Time Factors; D014475:Uncoupling Agents / Q000494:pharmacology; D014764:Viral Proteins / Q000276:immunology / Q000378:metabolism
chemical_list: D054328:Proton Pump Inhibitors; D017494:Proton Pumps; D014475:Uncoupling Agents; D014764:Viral Proteins; D000255:Adenosine Triphosphate; D011188:Potassium