Office: 141 Schweitzer Hall
117 Schweitzer Hall
University of Missouri
Columbia, MO 65211
|BS||Nanjing University||Nanjing, China||Biotechnology|
|PhD||University of Maryland, Baltimore County||Baltimore, Md.||Biochemistry|
Notable honors and service
Career Transition Award, Center for HIV RNA Studies (CRNA), 2013
The main research interest in our lab is to understand the structure of viral RNAs to begin to decipher the mechanism of viral replication. We utilize a variety of biophysical techniques including NMR spectroscopy and isothermal titration calorimetry. One of the projects consists of studying the structure of the 3´X tail of the Hepatitis C virus (HCV) genomic RNA and its role in regulating viral RNA replication. The highly conserved 98-nucleotide element on the 3 ́-end of the HCV genome is involved in the initiation of both viral RNA synthesis and protein translation. No homologous sequences have been observed in known cellular mRNAs, or in other RNA viruses, making it an ideal antiviral target. We are primarily using NMR spectroscopy to determine the structure of the 3´X, and investigate its interaction with the protein partners to gain insights into the structural basis for HCV RNA synthesis, and to provide molecular-level insights into a potential antiviral target.
The second project is to understand how host cellular factor RNA helicase A (RHA) influences HIV-1 viral protein translational control, and to determine the structural basis for RHA co-packaging into progeny virions. RHA assembles with genomic RNAs in HIV-1 viral particles and enhances viral infectivity. It interacts with the HIV-1 5 ́-untranslated region (5 ́-UTR), a highly conserved region of the genome that directs packaging during virus assembly. In addition to its assembly into virions, RHA activates viral protein synthesis by recognizing and binding to a Post-transcriptional Control Element (PCE) that is also located within the 5 ́-UTR. Using NMR spectroscopy combined with other in vitro techniques, we will characterize the interaction between the HIV-1 5´-UTR and RHA, and understand the regulation of HIV-1 translation and packaging.
Barton S, Heng X, Johnson BA, Summers MF. Database proton NMR chemical shifts for RNA signal assignment and validation. J Biomol NMR. 55:33-46 (2013).
Heng, X., Kharytonchyk, S., Garcia, E. L., Lu, K., Divakaruni, S. S., LaCotti, C., Edme, K., Telesnitsky, A., and Summers, M. F. Identification of a minimal region of the HIV-1 5'-leader required for RNA dimerization, NC binding, and packaging. J Mol Biol. 417, 224-239 (2012).
Lu, K., Heng, X., Garyu, L., Monti, S., Garcia, E. L., Kharytonchyk, S., Dorjsuren, B., Kulandaivel, G., Jones, S., Hiremath, A., Divakaruni, S. S., LaCotti, C., Barton, S., Tummillo, D., Hosic, A., Edme, K., Albrecht, S., Telesnitsky, A. & Summers, M. F. NMR detection of structures in the HIV-1 5'-leader RNA that regulate genome packaging. Science. 334, 242-5 (2011).