Probing Ebola VP35 Viral Protein Structures by Chemical Cross-linking and Mass Spectrometry
Document Type
Presentation
Abstract
Ebola virus (EBOV) infections show a fatality rate of 50% to 90% in humans. More specifically, multifunctional viral protein VP35 plays major role in viral replication, RNA silencing suppression, RNA-dependent protein kinase (PKR) inhibition, and ucleocapsid formation. The C-terminal domain binds viral RNA and sequesters it from host pattern recognition receptors and binds the host protein PACT that inhibits the interferon induction pathway. The N-terminal domain is thought to be involved in viral replication and oligomerization of the full length VP35 but mechanisms of these functions are not fully understood. Understanding how the protein oligomerizes and influences replication can elucidate therapeutic targets for controlling infection. Here, the applications of cross-linking and mass spectrometry approaches are presented for probing Ebola VP35 protein structure.
Publication Date
4-25-2017
Recommended Citation
Chanthamontri, Ken, "Probing Ebola VP35 Viral Protein Structures by Chemical Cross-linking and Mass Spectrometry" (2017). Faculty Symposium. 15.
https://digitalcommons.lindenwood.edu/faculty_symposium/15