Digitized Honors Theses (2002-2017)

Date of Award

5-2007

Document Type

Undergraduate Thesis

Degree Name

BS

Department

Biological Science

Faculty Mentor

Sailen Barik

Abstract

Cytoskeletal actin has been documented to play a necessary role in then transcriptional activities of respiratory syncytial virus (RSV). In order to map the transcriptional domains of actin utilized by the virus, we performed mutational analysis on recombinant actin to determine the functionality of each domain. This discourse attempted to determine mutual binding sites between viral particles and domains that actin utilizes for normal cell function. Using site-directed mutagenesis, point mutations and deletions were inserted into the following actin gene expressing protein domains: the highly acidic N-terminus, the divalent cation-bindi ng site, the nucleotide-bi nding site, and profilin binding sites. Activity of these mutant actin samples were assayed in a reconstituted RSV transcriptional system in vitro to test for productivity of the knockout domains. We determined that the divalent-cation binding site, highly acidic N-terminus, and profilin binding site were individually, in some fashion, responsible for normal RSV transcription while the nucleotide-binding site does not interact with RSV particles during transcription.

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