Poster abstracts
Poster number 135 submitted by Michele Tolbert
High Resolution RNA Solution Structure of the Stem Loop II Domain of the Enterovirus 71 Internal Ribosome Entry Site
Michele Tolbert (Department of Chemistry, Case Western Reserve University), Christopher E. Morgan (Department of Chemistry, Case Western Reserve University), Blanton S. Tolbert (Department of Chemistry, Case Western Reserve University)
Abstract:
Enterovirus 71 (EV71) is the major etiological agent involved in hand, foot and mouth disease. Infection is often acute, and may result in severe neurological and/or cardiovascular complications that can lead to severe morbidity and death. There currently are no vaccines or antivirals to help prevent infection or spread of disease, thus underscoring an urgent need to better understand the molecular mechanisms of this serious threat to public health. EV71 is a positive sense, single stranded RNA virus belonging to the Picorniavirdae family. Similar to other picornaviruses, EV71 utilizes a type I Internal Ribosome Entry Site (IRES) to promote viral translation. Type I IRES elements utilize structured domains to recruit host factors, which facilitate ribosomal loading via poorly understood mechanisms. Previous work from our group has shown that interactions between host hnRNP A1 and Stem Loop II (SLII) of the EV71 IRES is necessary for viral translation and replication, thus highlighting SLII as a critical region in the EV71 genome. To better understand the molecular determinants involved in SLII:hnRNP A1 interactions, a high resolution solution structure of the free SLII domain was solved using an integrated NMR and SAXS based approach. Herein, I will discuss the structural and thermodynamic implications involved in hnRNP A1 recognition of SLII.
Keywords: IRES, NMR, EV71