Professional Interests
The focus of Mamuka Kvaratskhelia’s laboratory research is to understand HIV replication, cancer development and DNA repair processes at the molecular level. The knowledge obtained will be exploited to develop new, highly effective anti-viral and anti-cancer drugs. They primarily use mass spectrometry as both a proteomic and structural biology tool to elucidate the composition and architecture of key biological macromolecules. In particular, powerful mass spectrometric methodologies are being developed to obtain high-resolution structural information on protein-nucleic acid, protein-protein and drug-protein complexes. Proteomic applications in our laboratory include dissection of human proteins participating in HIV replication, revealing essential posttranslational modifications in proteins, discovery of biomarkers for the early detection of cancer and identification of factors responsible for anti-cancer drug resistance. They augment our structural and proteomic studies with traditional biochemical, molecular biology and biophysical analysis to obtain a comprehensive picture of these important biological events.
Recent Publications
- Wang, H; Jurado, KA; Wu, X; Shun, MC; Li, X; Ferris, AL; Smith, SJ; Patel, PA; Fuchs, JR; Cherepanov, P; Kvaratskhelia, M; Hughes, SH; Engelman, A. HRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor. Nucleic acids research. 2012 Oct 5;
- Doueiri, R; Anupam, R; Kvaratskhelia, M; Green, KB; Lairmore, MD; Green, PL. Comparative host protein interactions with HTLV-1 p30 and HTLV-2 p28: insights into difference in pathobiology of human retroviruses. Retrovirology. 2012 Aug 9;9:64
- Larue, R; Gupta, K; Wuensch, C; Shkriabai, N; Kessl, JJ; Danhart, E; Feng, L; Taltynov, O; Christ, F; Van, Duyne, GD; Debyser, Z; Foster, MP; Kvaratskhelia, M. Interaction of the HIV-1 intasome with Transportin 3 (TNPO3 or TRN-SR2). The Journal of biological chemistry. 2012 Aug 7;
- Kessl, JJ; Jena, N; Koh, Y; Taskent-Sezgin, H; Slaughter, A; Feng, L; de, Silva, S; Wu, L; Le, Grice, SF; Engelman, A; Fuchs, JR; Kvaratskhelia, M. Multimode, cooperative mechanism of action of allosteric HIV-1 integrase inhibitors. The Journal of biological chemistry. 2012 May 11;287(20):16801-11
- Kessl, JJ; Li, M; Ignatov, M; Shkriabai, N; Eidahl, JO; Feng, L; Musier-Forsyth, K; Craigie, R; Kvaratskhelia, M. FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75. Nucleic acids research. 2011 Nov 1;39(20):9009-22
- Anupam, R; Datta, A; Kesic, M; Green-Church, K; Shkriabai, N; Kvaratskhelia, M; Lairmore, MD. Human T-lymphotropic virus type 1 p30 interacts with REGgamma and modulates ATM (ataxia telangiectasia mutated) to promote cell survival. The Journal of biological chemistry. 2011 Mar 4;286(9):7661-8
- Ranji, A; Shkriabai, N; Kvaratskhelia, M; Musier-Forsyth, K; Boris-Lawrie, K. Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs. The Journal of biological chemistry. 2011 Feb 18;286(7):5328-37
- Raghavendra, NK; Shkriabai, N; Graham, RLj; Hess, S; Kvaratskhelia, M; Wu, L. Identification of host proteins associated with HIV-1 preintegration complexes isolated from infected CD4+ cells. Retrovirology. 2010 Aug 11;7:66
- Kessl, JJ; McKee, CJ; Eidahl, JO; Shkriabai, N; Katz, A; Kvaratskhelia, M. HIV-1 Integrase-DNA Recognition Mechanisms. Viruses. 2009 Dec;1(3):713-36
- Kessl, JJ; Eidahl, JO; Shkriabai, N; Zhao, Z; McKee, CJ; Hess, S; Burke, TR, Jr; Kvaratskhelia, M. An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule. Molecular pharmacology. 2009 Oct;76(4):824-32
Education
- Postdoctoral Fellowships: Biological Chemistry Department of John Innes Center, England, UK; Biochemistry Department of the Dundee University, Scotland, UK and HIV Drug Resistance Program of the National Cancer Institute, MD, USA.
- Ph.D., 1990, The Georgian Institute and the Biotechnology Center of the Moscow State University, Biochemistry (Chemical Enzymology)
