Class Year: G3
Hometown: Fairfax Station, VA
Undergraduate Education: BS/08 Biochemistry (Minor in Music)/Georgetown U
Research Interest: Structural determinants of retroviral capsid assembly
Advisor: Rebecca Craven, PhD
Graduate Program: Cell & Molecular Biology
Description: Shortly after budding from an infected cell, retroviruses undergo Gag cleavage to release capsid (CA) protein. The subsequent rearrangement of the particle interior from an incomplete Gag sphere to a closed, mature capsid is an essential step in the formation of infectious virions. This maturation process is highly sensitive to therapeutic intervention, but since maturation is not well understood, it is unclear how capsid-targeting drugs accomplish their functions. Therefore, the steps of mature capsid assembly and regions of CA that are important to the process must be delineated. Doing so will lead to a more complete comprehension of the retorviral ;life cycle, provide avenues to improve on antiviral therapies targeting the capsid, and improve understanding of the means through which resistance to inhibitors can arise.
Our studies have identified two surface-exposed, structurally conserved features of the CA protein, the β-hairpin (BH) and flexible loop (FL) which may control CA assembly. Though these regions are spatially distant in CA and do not directly interact, they appear to act cooperatively to mediate capsid assembly. We hypothesize that the BH and FL cooperate to influence the structure of the CA through subtle but long-range interactions that control the protein's ability to assemble into mature capsids or maintain capsid integrity.
12th Annual Symposium for Antiviral Drug Resistance, Hershey, PA
Penn State College of Medicine Graduate Research Forum, Hershey, PA (poster)
FASEB Virus Structure and Assembly meeting, Saxtons River, VT
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