Poster abstracts

Poster number 53 submitted by Samuel Rund

Probing RNA binding by the nucleoprotein from ebolavirus

Samuel S. Rund (Chemistry & Biochemistry, DePauw University), Jonathan M. Howard (Chemistry & Biochemistry, DePauw University), Sharon M. Crary (Chemistry & Biochemistry, DePauw University)

Abstract:
Ebolavirus is an enveloped, nonsegmented, negative-sense RNA virus. As such, its RNA genome must be tightly wrapped in nucleocapsid proteins to be replication competent; it is this ribonucleoprotein complex that is the template for the viral polymerase. The most abundant protein in the nucleocapsid, the nucleoprotein (NP), coats the entire ~19 kilobase genomic and antigenomic RNAs throughout the viral replication cycle. The mechanism by which NP encapsidates the RNA is unknown, however, it is likely that encapsidation is nucleated through interactions with specific non-coding regions at the 5\' end of the viral RNA. We have studied the interactions of the 5\' terminus of the antigenomic viral RNA with bacterially expressed soluble NP in vitro using electrophoretic mobility shift assays. Results from these binding experiments will be presented.

Keywords: Ribonucleoprotein, virus