Identification of the DNA Binding Surface on the SIRV Capsid Protein

• Published in: The FASEB Journal
• Main Authors: Allgaier, Hannah E, Taurog, Rebecca E., Johnson, John E., Rohlman, Christopher E, Szymczyna, Blair R.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2013
• Subjects: Iceland
• Online Access: http://dx.doi.org/10.1096/fasebj.27.1_supplement.1000.1

Viruses that infect archaea have a unique system of resilient capsid proteins that must assemble and protect the virus genome from the harsh conditions in which some of these organisms survive. The Sulfolobus islandicus rod shaped virus (SIRV), for instance, is a non‐enveloped virus of the Rudiviridae family that infects the thermophilic and acidophilic Sulfolobus archaea. Members of this virus family have been isolated from solfataric fields in Iceland, Italy and the United States (Yellowstone National Park). Since the capsid of the Rudiviridae viruses is resilient to high temperatures and low pH, the capsid structure has potential uses as a nanobuilding block in biotechnological applications. An understanding of the requirements for SIRV capsid assembly will aid in the design of such nanomaterials. The solution structure of the C‐terminal domain of the SIRV capsid protein reveals the domain to be a four‐helix bundle. We are currently employing solution state NMR techniques to investigate how this region of the capsid protein associates with the double stranded DNA genome, and to ultimately get clues about the mechanism of capsid assembly.