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Cassiah Smith-Cox, Ph.D.

 

Biochemistry 2010

Area of Doctoral Study: Biochemistry
Research Advisor: Michael F. Summers, Ph.D.
Undergraduate Institute: St. Mary’s College of Maryland

Current Position: Clinical Trials Results Analyst, ICF International (NIH Campus)

Description of Research

Inhibiting viral assembly is one approach to preventing the development of mature infectious viruses such as the Human Immunodeficiency Virus (HIV-1). The production and assembly of viral particles for typical retroviruses such as HIV-1 is mediated by the Gag protein. Localization of Gag at the plasma membrane is a critical step in viral assembly. Gag, which consists of four domains, matrix (MA), capsid (CA) and nucleocapsid (NC), is targeted to the cell membrane via myristylation of the N-termianl matrix protein in HIV-1 and other retroviruses alike. However, there are retroviruses whose N-termini of Gag are not myristylated, such as the Equine Infectious Anemia Virus (EIAV). Therefore, my aim is to investigate the mechanism for Gag membrane binding by doing structural analysis of EIAV MA using Nuclear Magnetic Resonance (NMR). Similar studies are being conducted with the Matrix protein of the Feline Immunodeficiency Virus (FIV). Seeing as FIV has similar features to HIV-1, and is a virus that gets myristylated, it could serve as a relevant animal model for retroviruses that infect humans.