Potential role of cellular ESCRT proteins in the STIV life cycle.
We are examining the archaeal virus STIV (Sulfolobus turreted icosahedral virus) in order to elucidate the details of its replication cycle and its interactions with its cellular host, Sulfolobus solfataricus. Infection of Sulfolobus by STIV initiates an unusual cell lysis pathway. One component of this pathway is the formation of pyramid-like structures on the surface of infected cells. Multiple seven-sided pyramid-like structures are formed on infected cells late in the STIV replication cycle. These pyramid-like structures are formed at sites where the Sulfolobus S-layer has been disrupted and through which the cellular membrane protrudes. It is through the pyramid-like structures that virus-induced cell lysis occurs in the final stages of the STIV replication cycle. The pathway and process by which these unusual lysis structures are produced appears to be novel to archaeal viruses and are not related to the well-characterized lysis mechanisms utilized by bacterial viruses. We are interested in elucidating both the viral and cellular components involved with STIV lysis of its infected cell. In particular, we are examining the potential role that Sulfolobus ESCRT (endosomal sorting complex required for transport)-like proteins play during viral infection and lysis. We hypothesize that STIV takes advantage of the Sulfolobus ESCRT machinery for virus assembly, transport and cellular lysis.
Department of Plant Sciences and Plant Pathology, and Thermal Biology Institute, Montana State University, Bozeman, MT 59717, USA.
Jamie C
JC
Snyder
Mark J
MJ
Young
D019843:Archaeal Proteins / Q000378:metabolism*; D023641:Archaeal Viruses / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D056827:Endosomal Sorting Complexes Required for Transport / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D016944:Sulfolobus / Q000648:ultrastructure / Q000821:virology*
D019843:Archaeal Proteins; D056827:Endosomal Sorting Complexes Required for Transport