title: Sulfolobus turreted icosahedral virus c92 protein responsible for the formation of pyramid-like cellular lysis structures.
abstract: Host cells infected by Sulfolobus turreted icosahedral virus (STIV) have been shown to produce unusual pyramid-like structures on the cell surface. These structures represent a virus-induced lysis mechanism that is present in Archaea and appears to be distinct from the holin/endolysin system described for DNA bacteriophages. This study investigated the STIV gene products required for pyramid formation in its host Sulfolobus solfataricus. Overexpression of STIV open reading frame (ORF) c92 in S. solfataricus alone is sufficient to produce the pyramid-like lysis structures in cells. Gene disruption of c92 within STIV demonstrates that c92 is an essential protein for virus replication. Immunolocalization of c92 shows that the protein is localized to the cellular membranes forming the pyramid-like structures.
authors.affiliation: Department of Plant Sciences, 119 Plant Bioscience Building, Montana State University, Bozeman, MT 59717, USA.
authors.forename: Jamie C
authors.initials: JC
authors.lastname: Snyder
authors.forename: Susan K
authors.initials: SK
authors.lastname: Brumfield
authors.forename: Nan
authors.initials: N
authors.lastname: Peng
authors.forename: Qunxin
authors.initials: Q
authors.lastname: She
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Young
mesh_terms: D023641:Archaeal Viruses / Q000502:physiology*; D002462:Cell Membrane / Q000648:ultrastructure* / Q000821:virology; D054884:Host-Pathogen Interactions; D008958:Models, Molecular; D016366:Open Reading Frames / Q000235:genetics / Q000502:physiology; D048229:Sulfolobus solfataricus / Q000648:ultrastructure / Q000821:virology*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly; D014779:Virus Replication
chemical_list: D014764:Viral Proteins