Glycosylation plays a crucial role in establishing healthy symbiotic bacterial colonization patterns, maintaining mucosal barriers to infection, regulating both adaptive and innate immunity, and in host-pathogen interactions. For example, we recently found that glycomic shifts in blood sera are conserved in experimental mouse sepsis models (1). Furthermore, we found that proteins associated with human sepsis undergo dramatic shifts in glycosylation upon induction (1). This data suggests both a common mechanism for bacterially induced sepsis, and an important role for glycans in this response. Our lab continues to use systems-based approaches to study the mechanisms underlying critical immune functions.
Our Areas of Focus
Host Glycomics Response to Pathogens
- Heindel, D.W.; Chen, S.; Aziz, P.V.; Chung, J.Y.; Marth, J.D.; Mahal, L.K. Glycomic analysis reveals a conserved response to bacterial sepsis induced by different bacterial pathogens. ACS Infectious Diseases, 2022. doi: 10.1021/acsinfecdis.2c00082. Formerly bioRxiv doi: 10.1101/2020.12.11.421610
- Heindel, D.W.; Koppolu, S.; Zhang, Y.; Kasper, B.; Meche, L.; Vaiana, C.A.; Bissel, S.J.; Carter, C.E.; Kelvin, A.A.; Zhang, B.; Zhou, B.; TChou, T.-W.; Lashua, L.; Ross, T.M.; Ghedin, E.; Mahal, L.K. Glycomic analysis of host-response reveals high mannose as a key mediator of influenza severity. Proc. Nat. Acad. Sci. U.S.A., 2020, 117, 26926-26935. doi: 10.1073/pnas.2008203117. Formerly bioRxiv doi: 10.1101/2020.04.21.054098
- Qin, R.; Meng, G.; Pushalkar, S.; Carlock, M.A.; Ross, T.; Vogel, C.; Mahal, L.K. Glycomic analysis identifies pre-vaccination markers of response to influenza vaccine, implicating the complement pathway. medRixv, 2022, doi: 10.1101/2022.02.09.22270754. In submission.
- Kumar, A.; Ishida, R.; Strilets, T.; Cole, J.; Lopez-Orozco, J.; Fayad, N.; Felix-Lopez, A.; Elaish, M.; Evseev, D.; Magor, K.; Mahal, L.K.; Nagata, L.; Evans, D.; Hobman, T. SARS-CoV-2 non-structural protein 1 inhibits the interferon response by causing depletion of key host signaling factors. Journal of Virology, 2021, 95, 13, e0026621. doi: 10.1128/jvi.00266-21
- Nguyen, L.; McCord, K.A.; Bui, D.T.; Bouwman, K.M.; Kitova, E.N.; Elaish, M.; Kumawat, D.; Daskhan, G.C.; Tomris, I.; Han, L.; Chopra, P.; Yang, T.-J.; Willows, S.D.; Mason, A.L.; Mahal, L.K.; Lowary, T.L.; West, L.J.; Hsu, S.-T.D.; Hobman, T., Tompkins, S.M.; Boons, G.-J.; de Vries, R.P.; Macauley, M.S.; Klassen, J.S. Sialic acid-dependent binding and viral entry of SARS-CoV-2. Nature Chemical Biology, 2022, 18, 81-90. doi: 10.1038/s41589-021-00924-1
- Wang, L.; Koppolu, S.; Chappell, C.; Moncla, B.J.; Hillier, S.L.; Mahal, L.K. Studying the effects of reproductive hormones and bacterial vaginosis on the glycome of lavage samples from the cervicovaginal cavity. PLoS One, 2015, 10, e0127021. doi: 10.1371/journal.pone.0127021
- Koppolu, S.; Wang, L.; Mathur, A.; Nigam, J.A.; Dezzutti, C.S.; Isaacs, C.; Meyn, L.; Bunge, K.E.; Moncla, B.J.; Hillier, S.L.; Rohan, L.C.; Mahal, L.K. Vaginal product formulation alters the innate anti-viral activity and glycome of cervicovaginal fluids with implications for viral susceptibility. ACS Infectious Disease, 2018, 4, 1613-1622. doi: 10.1021/acsinfecdis.8b00157
- Krishnamoorthy, L.; Bess, J.W.; Preston, A.B.; Nagashima, K.; Mahal, L.K. HIV-1 and microvesicles from T cells share a common glycome, arguing for a common origin. Nature Chem. Biol., 2009 5, 244-250. doi: 10.1038/nchembio.151
- Batista, B.S.; Eng, W.S.; Pilobello, K.T.; Hendricks-Muñoz, K.; Mahal, L.K. Identification of a conserved glycan signature for microvesicles. J. Proteome Res., 2011, 10, 4624-33. doi: 10.1021/pr200434y
- Liang, Y.; Eng, W.S.; Colquhoun, D.R.; Dinglasan, R.R.; Graham, D.R.; Mahal, L.K. Complex N-linked glycans serve as a determinant for exosome/microvesicle cargo recruitment. J. Biol. Chem., 2014, 289, 32526-37. doi: 10.1074/jbc.M114.606269
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The Canada Excellence Research Chairs (CERC) Program awards universities up to $10 million over seven years to support world‑renowned researchers and their teams to establish ambitious research programs at Canadian universities.
Located in beautiful Edmonton, Alberta, Canada, the Chemistry Department at the UofA is renown for its active research. It is one of the best equipped and well funded departments in Canada.
It is a glycomic technology developed in the Mahal Lab, provide a rapid analysis of the glycome (1-3). These microarrays utilize immobilized carbohydrate-binding proteins at high spatial density to give specific information on the repertoire of glycans present.
miRNA can be used to identify glycosylation enzymes and their corresponding glycans that drive disease states.
At the UofA, you do not have to find a supervisor in order to apply. The department has a process in place for students to find a supervisor and join a research group once they arrive to start their program. However, it is recommended for applicants to contact chemistry faculty members whose areas of research are of interest to you. Information about requirements and how to apply can be found here.