The Sulfolobus Turreted Icosahedral virus (STIV) is a lytic hyperthermophile virus that infects members of the Sulfolobus family within the kingdom Crenarchaeota of the domain Archaea. The cryo-electron microscope (Cryo-EM) image reconstruction of the virus shows a striking architectural resemblance to the mammalian adenovirus, the bacteriophage PRD1, and algal virus PBCV-1. Structural studies of the major capsid proteins of adenovirus, PRD1, and PBCV-1 have shown a strong possiblity of evolutionary relationship between these viruses. This proposal sets forth structural and biophysical studies aimed in characterizing STIV and identifying whether this virus can be evolutionary related to the above mentioned viruses. The identification of a virus phylogeny encompassing the three divisions of life is exciting and unprecedented. Characterization of STIV, and Archaea infecting viruses in general, will provide substantial insight into the biochemistry of Archaea, virus host relationship and evolution, and biochemical adaptations required for survival under extreme environments. Detailed characterization of Archaea viruses may also expand our knowledge of viral evolution.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32AI065071-03
Application #
7213323
Study Section
Special Emphasis Panel (ZRG1-F04B (20))
Program Officer
Park, Eun-Chung
Project Start
2005-04-01
Project End
2008-03-31
Budget Start
2007-04-01
Budget End
2008-03-31
Support Year
3
Fiscal Year
2007
Total Cost
$51,278
Indirect Cost
Name
Scripps Research Institute
Department
Type
DUNS #
781613492
City
La Jolla
State
CA
Country
United States
Zip Code
92037
Khayat, Reza; Fu, Chi-yu; Ortmann, Alice C et al. (2010) The architecture and chemical stability of the archaeal Sulfolobus turreted icosahedral virus. J Virol 84:9575-83
Khayat, Reza; Lander, Gabriel C; Johnson, John E (2010) An automated procedure for detecting protein folds from sub-nanometer resolution electron density. J Struct Biol 170:513-21