Judith Marie Phillips was born on May 26, 1979 in Ames, Iowa, an event that may have hastened the completion of her father's PhD. studies. She spent her childhood in Chester County, Pennsylvania, where she began her biology training by turning over rocks and identifying the creatures underneath. After graduating from Sanford School in Hockessin, Delaware, she attended Kenyon College, where she worked with professor Joan L. Slonczewski on pH-inducible genes in Escherichia coli and Helicobacter pylori before embarking on a senior thesis project with professor Elizabeth A. Ottinger on the binding of Src SH2 and SH3 domains to peptide analogs of the p130 Cas protein. Following her graduation from Kenyon in 2000, she thought that she had finished with research and entered the Cornell University College of Veterinary Medicine with the intention of going into private practice. The allure of the bench proved stronger than expected, and following a summer working with Dr. Kenneth Simpson on Helicobacter infection in cats as part of Cornell's Leadership Program for Veterinary Students, she enrolled in the newly-founded Dual D.V.M./Ph.D. program and joined the laboratory of professor Volker M. Vogt to study retrovirus assembly. She completed the D.V.M. program in 2006. Later that summer, she married Karl F. Newman of Cortland, New York, and the completion of her Ph.D. studies is currently being hastened by the impending arrival of their first child.
DVM/PhD, Cornell University
The retroviral structural polyprotein Gag protein is both necessary and sufficient for the assembly of virus-like particles. Full-length Gag initially assembles into a immature particle that matures during or shortly after particle release, when the viral protease activates and cleaves Gag at several sites. Purified RSV Gag can be assembled in vitro into particles identical to immature retroviral protein cores. The C-terminal 25 amino acids of the p10 domain of Gag, immediately upstream of the major protein-protein interaction domain CA, are required for correct immature assembly, but their role has not been defined. A crystal structure of the N-terminal domain (NTD) of CA extended to include the last 25 amino acids of p10 was published in 2004. This structure showed a symmetrical dimer with an extensive p10-CA interface, but the dimer was incompatible with well-supported models of retroviral structure in which the NTD of CA forms a hexamer. I have been able to demonstrate that the p10-CA interface exists in immature virus particles, but as a six-fold rather than a two-fold interaction. This is true for particles assembled in vitro from purified protein and for those produced by transduced cells. This work has been accepted for publication.
Publications & Presentations
Phillips JM, Murray PS, Murray D, Vogt VM. 2008. "A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice." EMBO J. Published online 10 April 2008; print publication pending.
Slonczewski JL, McGee DJ, Phillips J, Kirkpatrick C, Mobley HL. 2000. "pH-dependent protein profiles of Helicobacter pylori analyzed by two-dimensional gels." Helicobacter. 5(4):240-7.
Blankenhorn D, Phillips J, Slonczewski JL. 1999. "Acid- and Base-Induced Proteins during Aerobic and Anaerobic Growth of Escherichia coli Revealed by Two-Dimensional Gel Electrophoresis." Journal of Bacteriology. 181(7):2209-2216.
Cold Spring Harbor Meeting, Retroviruses, May 2003. Phillips JM and Vogt VM. Poster. Title: Assembly and budding of RSV Gag-leucine zipper proteins in avian cells.
Cold Spring Harbor Meeting, Retroviruses, May 2004. Phillips, JM and Vogt VM. Poster. Title: Investigation of dimeric RSV CA NTD structure using cysteine cross-linking.
Cold Spring Harbor Meeting, Retroviruses, May 2005. Phillips, JM and Vogt VM. Talk. Title: Interaction between the C-terminal part of p10 and the CA domain of RSV Gag is required for immature assembly.
Cold Spring Harbor Meeting, Retroviruses, May 2007. Phillips, JM and Vogt VM. Talk. Title: A molecular switch required for immature assembly of RSV leads to a six-fold domain swap in the immature virus particle.
American Society for Virology, July 2007. Talk. Authors and title as above.