The formations of large molecular complexes on cellular membranes play important roles in both health and disease. However, understanding the structure and function of these complexes in their native membrane environment is a significant challenge. One system of interest is the assembly of new HIV-1 viruses on the cell membrane of infected cells. The viral encoded protein, Gag, forms large lateral networks on the membrane surface nucleating a viral assembly site. In addition, the Gag protein binds the viral genomic RNA, effectively acting as an adaptor linking the genetic material to the lipid envelope.
Our research group has a broad range of expertise and is developing and using cutting edge biophysical techniques to study membrane-associated proteins. In collaboration with a renowned virology laboratory at the National Cancer Institute, we are elucidating the complex mechanisms by which HIV and other retroviruses assemble on lipid membranes.
This research offers access and opportunities in a number of world-class scientific facilities. Projects will be designed based on the Associate’s interests and expertise. NIST and the Center for Neutron Research provide techniques such as Neutron Reflectivity, SANS and x-ray scattering for structural characterization, SPR & impedance spectroscopy for functional and kinetic studies, and high performance computer clusters for multilevel coarse grain and atomistic simulations. The Institute for Bioscience and Biotechnology Research has a state-of-the art protein expression and labeling facility. Furthermore, the National Cancer Institute provides fluorescence and electron microscopy facilities allowing for GUV and in vivo, cell based experiments. The Associate will be expected to publish in peer-reviewed journals. The laboratory welcomes biologists, chemists, physicists, and engineers excited about performing interdisciplinary research.
Nanda H, et al: Biophysical Journal 99(8): 2516, 2010
Datta S, et al: Journal of Molecular Biology 406(2): 205, 2011
HIV; Neutron scattering; Virus assembly; Lipid membranes; Molecular dynamics; Surface plasmon resonance; Electrical impedence spectroscopy; Membrane proteins;