Poster abstracts

Poster number 48 submitted by Dominic Qualley

The Nucleocapsid Protein of Feline Immunodeficiency Virus is an Efficient Nucleic Acid Chaperone

Dominic Francis Qualley (Department of Chemistry and Biochemistry and the Center for Retrovirus Research), Karin Musier-Forsyth (Department of Chemistry and Biochemistry and the Center for Retrovirus Research)

Abstract:
Nucleic acid chaperone proteins facilitate DNA and RNA rearrangements resulting in a thermodynamically more stable conformation. In retroviruses, the small, highly basic nucleocapsid (NC) protein serves as a chaperone and facilitates many nucleic acid restructuring events in the retroviral life cycle. Feline immunodeficiency virus (FIV) is a retrovirus that naturally occurs in the domestic cat and produces symptoms similar to those found in HIV-infected humans. FIV is very similar to HIV in structure and pathology and is a useful animal model for the study of certain aspects of pathogenesis and for the evaluation of antiviral strategies. Furthermore, the use of FIV as a tool for gene therapy makes it a particularly attractive model system in which to test such approaches. Compared to HIV, little is known about the molecular determinants of FIV NC chaperone activity. In this work, we carry out biochemical and biophysical studies to investigate FIV NC’s chaperone function. Sedimentation assays were used to characterize NC-facilitated nucleic acid aggregation, gel mobility-shift assays measured NC-guided annealing of DNA/RNA, and fluorescence anisotropy experiments provided apparent Kd values for FIV NC binding to DNA and RNA constructs. Taken together, the studies carried out to date provide evidence that FIV NC protein shows chaperone activity similar to that of HIV NC. Future experiments are aimed at mutational analysis of FIV NC in vitro and in cell culture.

Keywords: retrovirus, nucleocapsid