Characterization of NFkB Inhibition by Poxviral Ankyrin/F-box Proteins

• Author / Creator

  Burles, Kristin A

• One of the most notable features of poxviruses is their ability to regulate cellular signaling pathways, including the ubiquitin-proteasome system. Ubiquitin plays a crucial role in the fate of a protein. Typically poly-ubiquitinated proteins are degraded by the 26S proteasome. The Skp1, culllin-1, F-box (SCF) ubiquitin ligase links ubiquitin to a substrate through a family of proteins possessing F-box domains. Recently, our lab has determined that ectromelia virus, the causative agent of lethal mousepox, encodes four F-box-containing proteins, ECTV002, ECTV005, ECTV154, and ECTV165, that interact with the SCF ubiquitin ligase. Many cellular pathways are tightly controlled by the SCF ubiquitin ligase, including the nuclear factor kappa B (NFκB) pathway, which mediates an antiviral immune response. We have shown that the ectromelia ankyrin/F-box proteins inhibit NFκB activation. Our data also suggest that ECTV002 and ECTV154 mediate virion release or spread.

• Subjects / Keywords

  • Poxvirus
  • NFkappaB
  • Ankyrin

• Graduation date

  Fall 2012

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R3NQ81

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.