Investigation of dengue virus RNA terminal region interactions with human host proteins

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dc.contributor.authorDemeler, Aysha K.
dc.contributor.authorUniversity of Lethbridge. Faculty of Arts and Science
dc.contributor.supervisorPatel, Trushar R.
dc.date.accessioned2025-11-21T16:53:20Z
dc.date.available2025-11-21T16:53:20Z
dc.date.issued2025
dc.degree.levelMasters
dc.description.abstractDengue virus (DENV) is a globally important arthropod-borne pathogen responsible for dengue fever, which can range from mild fever to severe hemorrhagic fever and shock syndrome. With no specific antiviral treatments available, understanding the molecular mechanisms of DENV replication and its interactions with host proteins is essential. This study focuses on two interconnected projects that use advanced biophysical techniques to address these challenges. The first project assesses biophysical methods for studying protein-protein interactions (PPIs) in solution, using the sfGFP-anti-GFP nanobody system as a model. Techniques such as microscale thermophoresis, fluorescence correlation spectroscopy, analytical ultracentrifugation, isothermal titration calorimetry, and size exclusion chromatography coupled with multi-angle light scattering were systematically compared. This analysis creates a reliable framework for studying PPIs, which can be applied to protein-RNA and RNA-RNA interactions. The second project examines the interaction between DENV serotype 2 (DENV-2) and the human DEAD-Box Helicase 6 protein (DDX6), a host factor involved in viral replication and assembly. By exploring the molecular interactions between the terminal regions of DENV-2 RNA and DDX6, this work aims to provide mechanistic insights into how DENV hijacks host proteins. To support these studies, DDX6 was expressed recombinantly with a superfolder green fluorescent protein (sfGFP) tag, which facilitates detection in fluorescence-based assays and improves protein yield. Collectively, these findings establish that DDX6 recognizes each structural domain of the DENV-2 3′ UTR independently. Through a robust biophysical framework, we demonstrated this interaction using multiple complementary techniques, extending detailed characterization to a domain that has not been previously studied in depth.
dc.embargoNo
dc.identifier.urihttps://hdl.handle.net/10133/7225
dc.language.isoen
dc.publisherLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry
dc.publisher.departmentDepartment of Chemistry and Biochemistry
dc.publisher.facultyArts and Science
dc.relation.ispartofseriesThesis (University of Lethbridge. Faculty of Arts and Science)
dc.subjectdengue virus
dc.subjectRNA terminal region
dc.subjecthuman host proteins
dc.subjectprotein-protein interactions
dc.subjectviral replication
dc.subject.lcshDissertations, Academic
dc.subject.lcshDengue viruses--Reproduction--Research
dc.subject.lcshRNA-protein interactions--Research
dc.subject.lcshMolecular virology
dc.subject.lcshCatalytic RNA--Research
dc.subject.lcshNon-coding RNA--Research
dc.titleInvestigation of dengue virus RNA terminal region interactions with human host proteins
dc.typeThesis
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