| Autor: |
Gruenke PR; Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States.; Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States.; Bond Life Sciences Center, University of Missouri, Columbia, Missouri 65211, United States., Mayer MD; Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States., Aneja R; Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States., Schulze WJ; Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States., Song Z; Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States., Burke DH; Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States.; Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States.; Bond Life Sciences Center, University of Missouri, Columbia, Missouri 65211, United States., Heng X; Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States., Lange MJ; Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States.; Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States. |
| Abstrakt: |
The HIV-1 capsid protein (CA) assumes distinct structural forms during replication, each presenting unique, solvent-accessible surfaces that facilitate multifaceted functions and host factor interactions. However, functional contributions of individual CA structures remain unclear, as evaluation of CA presents several technical challenges. To address this knowledge gap, we identified CA-targeting aptamers with different structural specificities, which emerged through a branched SELEX approach using an aptamer library previously selected to bind the CA hexamer lattice. Subsets were either highly specific for the CA lattice or bound both the CA lattice and CA hexamer. We then evaluated four representatives to reveal aptamer regions required for binding, highlighting interesting structural features and challenges in aptamer structure determination. Further, we demonstrate binding to biologically relevant CA structural forms and aptamer-mediated affinity purification of CA from cell lysates without virus or host modification, supporting the development of structural form-specific aptamers as exciting new tools for the study of CA. |
