Proteomic Analysis of Sulfolobus solfataricus during Sulfolobus Turreted Icosahedral Virus Infection

• Published in: Journal of proteome research Vol. 11; no. 2; pp. 1420 - 1432
• Main Authors: Maaty, Walid S, Selvig, Kyla, Ryder, Stephanie, Tarlykov, Pavel, Hilmer, Jonathan K, Heinemann, Joshua, Steffens, Joseph, Snyder, Jamie C, Ortmann, Alice C, Movahed, Navid, Spicka, Kevin, Chetia, Lakshindra, Grieco, Paul A, Dratz, Edward A, Douglas, Trevor, Young, Mark J, Bothner, Brian
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 03-02-2012
• Subjects: Amino Acid Sequence; Archaeal Proteins - analysis; Archaeal Proteins - chemistry; Archaeal Proteins - metabolism; Archaeal Viruses - genetics; Archaeal Viruses - metabolism; Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional; Host-Pathogen Interactions; Molecular Sequence Data; Proteomics - methods; Sequence Alignment; Sulfolobus solfataricus - chemistry; Sulfolobus solfataricus - metabolism; Sulfolobus solfataricus - virology; Tandem Mass Spectrometry; Virus Replication; 2-D fluorescence difference gel electrophoresis; liquid chromatography mass spectrometry, LC−MS/MS; differential gene expression; virus-associated pyramids, VAPs; virus−host interaction; proteomics; thiol-reactive maleimide probe; Archaea; Sulfolobus turreted icosahedral virus, STIV; membrane protein; Sulfolobus solfataricus strain P2; virus infection
• ISSN: 1535-3893; 1535-3907
• DOI: 10.1021/pr201087v

Where there is life, there are viruses. The impact of viruses on evolution, global nutrient cycling, and disease has driven research on their cellular and molecular biology. Knowledge exists for a wide range of viruses; however, a major exception are viruses with archaeal hosts. Archaeal virus–host systems are of great interest because they have similarities to both eukaryotic and bacterial systems and often live in extreme environments. Here we report the first proteomics-based experiments on archaeal host response to viral infection. Sulfolobus Turreted Icosahedral Virus (STIV) infection of Sulfolobus solfataricus P2 was studied using 1D and 2D differential gel electrophoresis (DIGE) to measure abundance and redox changes. Cysteine reactivity was measured using novel fluorescent zwitterionic chemical probes that, together with abundance changes, suggest that virus and host are both vying for control of redox status in the cells. Proteins from nearly 50% of the predicted viral open reading frames were found along with a new STIV protein with a homologue in STIV2. This study provides insight to features of viral replication novel to the archaea, makes strong connections to well-described mechanisms used by eukaryotic viruses such as ESCRT-III mediated transport, and emphasizes the complementary nature of different omics approaches.