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Like all retroviruses, FeLV encodes the structural polyprotein Gag, which plays a significant role in genomic RNA packaging and virion assembly, making it a critical target for antiviral studies. Despite its importance, structural and biochemical studies of FeLV have been limited by the lack of an efficient purification strategy. In this study, recombinant FeLV Gag was expressed in Escherichia coli BL21-CodonPlus(DE3) cells and purified using affinity-based chromatographic techniques. Initial purification using Ni2+ affinity chromatography confirmed protein expression at the expected molecular weight but revealed significant limitations in both protein recovery and purity. Optimization of lysis conditions improved recovery of soluble FeLV Gag. Purification by Ni2+ affinity chromatography yielded protein at concentrations ~200 μM, sufficient for preliminary studies; however, sample purity remained insufficient for downstream structural applications. Additional purification strategies, including ion-exchange and heparin affinity chromatography, improved selectively but did not fully resolve contaminating proteins. These results demonstrate that while expression of FeLV Gag can be reliably achieved and adequate protein concentration can be obtained, purification remains the primary limitation in procuring material suitable for structural and biophysical characterization. Further optimization of chromatographic approaches, including size-exclusion chromatography, is expected to improve sample purity for downstream applications such as bio-layer interferometry (BLI) and Small-angle X-ray scattering (SAXS)."},{"label":"Format","value":["application/pdf"]},{"label":"Language","value":["English"]},{"label":"Language (DLG)","value":["eng"]},{"label":"Publisher","value":["Berry College"]},{"label":"Medium","value":["theses"]},{"label":"Extent","value":"23 pages"},{"label":"Holding Institution","value":["Berry College"]},{"label":"Type","value":["Text"]},{"label":"Decade","value":["2020s"]},{"label":"Rights","value":["In Copyright"]},{"label":"Rights Link","value":"<a href=\"https://rightsstatements.org/page/InC/1.0/?language=en\" target=\"_blank\"> In Copyright</a>"},{"label":"Rightsholder","value":["Nikki L. Crummey"]},{"label":"Access Restrictions","value":["immediate unrestricted access"]},{"label":"Subject","value":["Feline leukemia virus"]},{"label":"School","value":["School of Mathematical and Natural Sciences"]},{"label":"Department","value":["Chemistry and Biochemistry"]},{"label":"Author","value":["Nikki L. Crummey"]},{"label":"Author Supplied Keywords","value":"Retrovirus Gag, Protein purification, Ni²⁺ affinity chromatography, Ion-exchange chromatography, Viral assembly, Feline leukemia virus"},{"label":"Research Funding","value":["Summer Undergraduate Research Fellowship"]},{"label":"Research Funding Link","value":"Learn more about <a href=\"https://berry.edu/academics/faculty-resources/undergraduate-research/summer-research\" target=\"_blank\"> summer research. </a>"},{"label":"Project Type","value":["Thesis"]},{"label":"Degree","value":["Bachelor of Science"]},{"label":"Committee Chair","value":["Dominic Qualley"]},{"label":"Faculty Advisor","value":["Savannah Post"]},{"label":"Major","value":["Chemistry"]}],"description":"Purification and Properties of the Feline Leukemia Virus Gag 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