Analysis of human fluids by NMR:

• Quantification of blood acute-phase inflammation proteins and thereof glycosylation profiles (Proteo-metabolomics).
• Development of new computational tools in metabo-proteomics for clinical purposes.

NMR studies into carbohydrate glycan interactions:

• Identification of mechanisms of glycan metabolism by bacteria inhabiting the human gut microbiome.
• Binding of Norovirus to Histo Blood Group antigens and related glycans found in human tissues and fluids.

Publications

1. Mallagaray, A., Rudolph, L., Lindloge, M., Mölbitz, J., Thomsen, H., Schmelter, F., Alhabash, M.W., Abdullah, M.R., Sarei, R., Ehlers, M., Graf, T., Sina, C., Petersmann, A., Nauck, M., Günther, U.L. (2023) Towards a precise NMR quantification of acute phase inflammation proteins from human serum. Angewandte Chemie International Edition, e202306154. https://doi.org/10.1002/anie.202306154
2. Trastoy, B, Du, J.J., Cifuente, J.O., Rudolph, L., García-Alija, M., Klontz, E.H., Deredge, D., Sultana, N., Huynh, C.G., Flowers, M.W., Li, C., Sastre, D.E., Lai-Xi, W., Corzana, F., Mallagaray, A., Sundberg, E.J., Guerin, M.E. (2023) Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases. Nature Communications, 14, 1705. https://doi.org/10.1038/s41467-023-37215-3
3. Creutznacher, R., Schulze-Niemand, E., König, P., Stanojlovic, V., Mallagaray, A., Peters, T., Stein, M., Schbert, M. (2023) Conformational control of fast asparagine deamidation in a norovirus capsid protein. Biochemistry, 62, 1032-1043. https://doi.org/10.1021/acs.biochem.2c00656
4. Maass, T., Ssebyatika, G., Brückner, M., Breckwoldt, L., Krey, T., Mallagaray, A., Peters, T., Frank, M., Creutznacher, R. (2022) Binding of glycans to the SARS CoV-2 spike protein, an open question: NMR data on binding site localization, affinity, and selectivity. Chemistry – A European Journal, e202202614, https://doi.org/10.1002/chem.202202614
5. Mühlberg, L., Alarcin, T., Maass, T., Creutznacher, R., Küchler, R., Mallagaray, A. (2022) Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins. Journal of Biomolecular NMR, 76, 59-74. https://doi.org/10.1007/s10858-022-00394-0
6. Creutznacher, R., Maass, T., Dülfer, J., Feldmann, C., Hartmann, V., Lane, M. S., Knickmann, J., Westermann, L. T., Thiede, L., Smith, T. J., Uetrecht, C., Mallagaray, A., Waudby, C. A., Taube, S., Peters, T. (2022) Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions. Communications Biology, 5, article number 563. https://doi.org/10.1038/s42003-022-03497-4
7. Peters, T., Creutznacher, R., Maass, T., Mallagaray, A., Ogressik, P., Taube, S., Thiede, L., Uetrecht, C. (2022) Norovirus-glycan interactions – how strong are they really? Biochemical Society Transactions 50, 347-359. https://doi.org/10.1042/BST20210526
8. Khilji, S. K., Goerdeler, F., Frensemeier, F., Warschkau, D., Lühle, J., Fandi, Z., Schirmeister, F., Chen, Z. A., Turak, O., Mallagaray, A., Boerno, S., Timmerman, B., Rappsilber, B., Seeberger, P.H., Moscovitz, O. (2022) Generation of glycan-specific nanobodies. Cell Chemical Biology, 29, 1353-1361.e6. https://doi.org/10.1016/j.chembiol.2022.05.007
9. Maass T, Westermann LT, Creutznacher R, Mallagaray A, Dülfer J, Uetrecht C, Peters T (2022) Assignment of Ala, Ile, LeuProS, Met and ValProS methyl groups of the protruding domain of murine norovirus capsid protein VP1 using methyl-methyl NOEs, site directed mutagenesis and pesudocontact shifts. Biomolecular NMR Assignments, 16, 97-107. https://doi.org/10.1007/s12104-022-10066-7
10. Creutznacher, R., Maass, T., Ogressik, P., Wallmann, G., Feldmann, C., Peters, H., Lingemann, M., Taube, S., Peters, T., Mallagaray, A. (2021) NMR experiments shed new light on glycan recognition by human and murine norovirus capsid proteins. Viruses, 13, 416-434. https://doi.org/10.3390/v13030416
11. Yan, H., Lockhauserbäumer, J., Szekeres, G. P., Mallagaray, A., Creutznacher, R., Taube, S., Peters, T., Pagel, K., Uetrecht, C. (2021) Protein secondary structure affects glycan clustering in native mass spectrometry. Life, 11, 554-568. https://doi.org/10.3390/life11060554
12. Schmelter, F., Föh, B., Mallagaray, A., Rahmöller, J., Ehlers, M., Lehrian, S., Kopylow, V.v., Künstig, I., Lixenfeld, A.S., Martin, E., Ragab, M., Borsche, M., Balck, A., Vollstedt, E.J., Meyer-Saraei, R., Kreutzmann, F., Eitel, I., Taube, S., Klein, C., Katalinic, A., Rupp, J., Jantzen, E., Graf, T., Sina, C., Günther, U.L. (2021) Metabolic markers distinguish COVID-19 from other intensive care patients and show potential to stratify for disease risk. Frontiers in Molecular Biosciences https://doi.org/10.3389/fmolb.2021.737039
13. Dülfer, J., Yan, H., Brodmerkel, M.N., Creutznacher, R., Mallagaray, A., Peters, T., Caleman, C., Marklund, E.G., Uetrecht, C. (2021) Glycan-induced protein dynamics in human norovirus P dimers depend on virus strain and deamidation status. Molecules, 26, 2125-2149. https://doi.org/10.3390/molecules26082125
14. Mende, M., Tsouka, A., Heidepriem, J., Paris, G., Mattes, D.S., Eickelmann, S., Bordoni, V., Wawrzinek, R., Fuchsberger, F., Seeberger, P.H., Rademacher, C., Delbianco, M., Mallagaray, A., Loeffler, F.F. (2020) On-Chip Neo-Glycopeptide synthesis for multivalent glycan presentation. Chem. Eur. J., 26, 9954-9963. https://doi.org/10.1002/chem.202001291
15. Müller-Hermes, C., Creutznacher, C., Mallagaray, A. (2020) Complete assignment of Ala, Ile, Leu^ProS, Met and Val^ProS methyl groups of the protruding domain from human Norovirus GII.4 Saga. Biomolecular NMR Assignments, 14, 123-130. https://doi.org/10.1007/s12104-020-09932-z
16. Creutznacher, R., Schulze, E., Wallman, G., Peters, T., Stein, M., Mallagaray, A. (2020) Chemical-shift perturbations reflect bile acid binding to Norovirus coat protein: recognition comes in different flavours. ChemBioChem, 21, 1007-1021. https://doi.org/10.1002/cbic.201900572
17. Mallagaray, A., Creutznacher, R., Dülfer, J., Mayer, P.H.O., Grimm, L.L., Orduña, J.M., Trabjerg, E., Stehle, T., Rand, K.D., Blaum, B.S., Uetrecht, C., Peters, T. (2019) A post-translational modification of human Norovirus capsid protein attenuates glycan binding. Nature Communications,  10, Article number: 1320. https://doi.org/10.1038/s41467-019-09251-5
18. Bücher, K.S., Yan, H., Creutznacher, R., Ruoff, K., Mallagaray, A., Grafmüller, A., Dirks, J.S., Kilic, T., Weickert, S., Rubailo, A., Drescher, M., Schmidt, S., Hansman, G., Peters, T., Uetrecht, C., Hartmann, L. (2018) Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid protein, BioMacromolecules, 19, 3714-3724. https://doi.org/10.1021/acs.biomac.8b00829

Eric J. Sundberg (Emory University School of Medicine, USA)