Open AccessSulfolobus Turreted Icosahedral Virus c92 Protein Responsible for the Formation of Pyramid-Like Cellular Lysis Structures
Author(s) -
Jamie C. Snyder,
Susan K. Brumfield,
Nan Peng,
Qunxin She,
Mark Young
Publication year - 2011
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00379-11
Subject(s) - sulfolobus solfataricus , biology , sulfolobus , icosahedral symmetry , archaea , pyramid (geometry) , open reading frame , lysis , virus , dna virus , gene , virology , genetics , peptide sequence , microbiology and biotechnology , genome , crystallography , chemistry , physics , optics
Host cells infected bySulfolobus 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 inArchaea 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 hostSulfolobus solfataricus . Overexpression of STIV open reading frame (ORF) c92 inS. 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.