I am a Postdoctoral Associate in the laboratory of Dr. Mohsan Saeed in the Department of Biochemistry at Boston University School of Medicine. Before joining the Saeed lab, I did my M. Phil in Biochemistry at the International Center for Chemical and Biological Sciences, Pakistan, and Ph.D. at the Max Planck Institute for Biophysical Chemistry, Germany. During my Ph.D., I performed biochemical and biophysical analysis of human nucleotide kinases and devised strategies to enhance the ability of these kinases to activate nucleoside-analog prodrugs with antiviral and anticancer properties.
My current research explores the role of human proteases in viral infections. A human cell is estimated to contain approximately 600 proteases and protease-inhibiting proteins that work in concert with each other to orchestrate various biological processes, such as cell-cycle progression, cell proliferation, DNA replication, and tissue remodeling. In addition, cellular proteases have been shown to have important roles in virus infection, as evidenced by ACE2, TMPRSS2, CTSL, and DPP4 being critical host dependency factors for coronavirus replication. I utilize protein overexpression and depletion strategies to systematically analyze the role of cellular proteases in various steps of coronavirus infection. Once the candidate genes are identified, I take multidisciplinary approaches combining virology, molecular biology, biochemistry, and structural analyses to uncover the mechanisms through which cellular proteases contribute to virus infection.
Publications
1. Chen, D.-Y., Khan, N., Close, B. J., Goel, R. K., Blum, B., Tavares, A. H., Kenney, D., Conway, H. L., Ewoldt, J. K., Chitalia, V. C., Crossland, N. A., Chen, C. S., Kotton, D. N., Baker, S. C., Fuchs, S. Y., Connor, J. H., Douam, F., Emili, A., & Saeed, M. (2021). SARS-COV-2 disrupts proximal elements in the Jak-Stat Pathway. Journal of Virology, 95(19). https://doi.org/10.1128/jvi.00862-21
2. Bandyopadhyay, S., Douglass, J., Kapell, S., Khan, N., Feitosa-Suntheimer, F., Klein, J. A., Temple, J., Brown-Culbertson, J., Tavares, A. H., Saeed, M., & Lau, N. C. (2021). DNA templates with blocked long 3ʹ end single-stranded overhangs (bl3sso) promote bona fide cas9-stimulated homology-directed repair of long transgenes into endogenous gene loci. G3 Genes|Genomes|Genetics, 11(8). https://doi.org/10.1093/g3journal/jkab169
3. Khan, N., Shah, P. P., Ban, D., Trigo-Mouriño, P., Carneiro, M. G., DeLeeuw, L., Dean, W. L., Trent, J. O., Beverly, L. J., Konrad, M., Lee, D., & Sabo, T. M. (2019). Solution structure and functional investigation of human guanylate kinase reveals allosteric networking and a crucial role for the enzyme in cancer. Journal of Biological Chemistry, 294(31), 11920–11933. https://doi.org/10.1074/jbc.ra119.009251
4. Khan, N., Park, J., Dean, W. L., Gray, R. D., Tse, W., Lee, D., & Sabo, T. M. (2020). Recombinant expression and purification of af1q and its interaction with T-cell factor 7. Protein Expression and Purification, 165, 105499. https://doi.org/10.1016/j.pep.2019.105499
5. Khan, N., Ban, D., Trigo-Mourino, P., Carneiro, M. G., Konrad, M., Lee, D., & Sabo, T. M. (2017). 1H, 13C and 15N resonance assignment of human Guanylate kinase. Biomolecular NMR Assignments, 12(1), 11–14. https://doi.org/10.1007/s12104-017-9771-6
6. Jain, R., Khan, N., Menzel, A., Rajkovic, I., Konrad, M., & Techert, S. (2015). Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering. European Biophysics Journal, 45(1), 81–89. https://doi.org/10.1007/s00249-015-1079-9
7. Donatan, S., Yashchenok, A., Khan, N., Parakhonskiy, B., Cocquyt, M., Pinchasik, B.-E., Khalenkow, D., Möhwald, H., Konrad, M., & Skirtach, A. (2016). Loading capacity versus enzyme activity in anisotropic and spherical calcium carbonate microparticles. ACS Applied Materials & Interfaces, 8(22), 14284–14292. https://doi.org/10.1021/acsami.6b03492
8. Sabir, N., Khan, N., Völkner, J., Widdascheck, F., del Pino, P., Witte, G., Riedel, M., Lisdat, F., Konrad, M., & Parak, W. J. (2015). Photo-electrochemical bioanalysis of guanosine monophosphate using coupled enzymatic reactions at a cds/zns quantum dot electrode. Small, 11(43), 5844–5850. https://doi.org/10.1002/smll.201501883
