Bridging Resolutions: New Insights In Structural Virology From Cryo-Correlative Light and Electron
|Speaker:||Elizabeth R. Wright
||Wednesday, February 22, 2017
||1:30pm - 2:30pm
||Schiciano Auditorium Side B, FCIEMAS, Duke
||Registration required: http://bit.ly/2kofTBW
Developments in technologies surrounding cryo-EM and light microscopy have transformed the fields of correlative microscopy and structural virology. It is now possible to achieve atomic and near atomic resolution structures of macromolecular complexes and viruses via cryo-EM and cryo-ET. In addition, technologies have provided a means for probing the spatiotemporal landscapes of cells and viruses at high resolution and in four-dimensions. My laboratory uses cryo-EMand molecular biology approaches to explore the three-dimensional (3D) structures of viruses and cells. In this talk, I will discuss some of our contributions to the fields of electron microscopy and structural virology. In particular, I will present data on our cryo-EM structural investigations of pleomorphic enveloped viruses, namely respiratory syncytial virus (RSV) and measles virus. I will also present results of our cryo-EM methods development as applied to studies of viruses and cells. I will conclude by briefly outlining some of our future directions and challenges facing the field.
Elizabeth Wright received her B.S. in Biology and Chemistry from Columbus State University, Columbus, GA in 1995 and 1997, respectively. She received her Ph.D. from the Department of Chemistry at Emory University, Atlanta, GA in 2002. She was a postdoctoral associate in the laboratory of Professor Anupam Madhukar at the University of Southern Californiato develop approaches for bridging nanoscale biological and quantum-based materials. From there, she was a postdoctoral scholar in the cryo-EM laboratory of Professor Grant Jensen at Caltech. During that time, she received an NIH NRSA postdoctoral fellowship to study the 3D structure of HIV. While there, she determined the 3D structure of the immature virus and proposed that six-helix bundles formed by the SP1 domain of the Gag polyprotein stabilize the immature capsid protein lattice. In 2008, she joined the faculty at Emory University in the Department of Pediatrics. She is also the director of the University-wide EM facility. She has pioneered the development and application of numerous technologies including: affinity grid methods for capturing viruses and other complexes on EM grids; self-pressurized rapid freezing and CEMOVIS of bacteria; conventional and cryo-preservation methods for structural studies of the lipopolysaccharide (LPS) and capsular polysaccharide (capsule) of bacteria; enhanced phase contrast (both Zernike and hole-free) cryo-EM/cryo-ET; and cryo-correlative light and electron microscopy (cryo-
CLEM) methods for studying bacteria, virus, and eukaryotic cell structure and function. Her present work is focused on structural studies of pathogenic enveloped viruses and bacteria, as well as the
development of methods for improving correlative structural biology.