Structural Analysis of the CVB3 Genomic 5' UTR
Advisor Information
William Tapprich
Location
225
Presentation Type
Oral Presentation
Start Date
1-3-2019 12:45 PM
End Date
1-3-2019 2:00 PM
Abstract
Coxsackievirus B3 (CVB3) is an important human pathogen and has been determined as a causative agent of myocarditis and pancreatitis. The single-stranded, positive-sense genomic RNA of CVB3 serves as a template for the production of the viral structural and nonstructural proteins. In absence of an m7G cap, the viral RNA has to rely on cap-independent translation initiation mechanisms. Similar to other enteroviruses, the CVB3 genome has a long, highly structured 5’ untranslated region (UTR), which has been identified as a determinant of viral virulence. The 5’ UTR houses a cloverleaf-like structure and a type I internal ribosome entry site, the proper folding of which is necessary for the interactions of the 5’ UTR with viral and host trans-acting factors and underlines the efficiency of viral replication. Here, we utilized a chemical probing method to characterize the secondary structure of the CVB3 5’ UTR. We propose a model with novel structural features including realignment of major domains and newly identified long-range interactions. Taken together, our work brings us closer to bridging the gap between structure and function in processes essential for the replicative success of CVB3 and related enteroviruses.
Structural Analysis of the CVB3 Genomic 5' UTR
225
Coxsackievirus B3 (CVB3) is an important human pathogen and has been determined as a causative agent of myocarditis and pancreatitis. The single-stranded, positive-sense genomic RNA of CVB3 serves as a template for the production of the viral structural and nonstructural proteins. In absence of an m7G cap, the viral RNA has to rely on cap-independent translation initiation mechanisms. Similar to other enteroviruses, the CVB3 genome has a long, highly structured 5’ untranslated region (UTR), which has been identified as a determinant of viral virulence. The 5’ UTR houses a cloverleaf-like structure and a type I internal ribosome entry site, the proper folding of which is necessary for the interactions of the 5’ UTR with viral and host trans-acting factors and underlines the efficiency of viral replication. Here, we utilized a chemical probing method to characterize the secondary structure of the CVB3 5’ UTR. We propose a model with novel structural features including realignment of major domains and newly identified long-range interactions. Taken together, our work brings us closer to bridging the gap between structure and function in processes essential for the replicative success of CVB3 and related enteroviruses.