Dr. Stephen Evans

Research interests

Identifying and exploiting structure-function relationships in carbohydrate-active enzymes and carbohydrate-binding proteins using structure determination by single-crystal X-ray diffraction, Surface Plasmon Resonance, Isothermal Calorimetry, and computer-assisted molecular modeling.

 

Recent publications

Legg, M.S.G., Gagnon, S.M.L., Powell, C.J., Boulanger, M.J., Li, A.J.J. & Evans, S.V. (2022) Monoclonal antibody 7H2.2 binds the C-terminus of the cancer-oocyte antigen SAS1B through the hydrophilic face of a conserved amphipathic helix corresponding to one of only two regions predicted to be ordered. Acta Crystallogr. D Struct. Biol. 78, 623-632.

Blackler R.J., Müller-Loennies S., Pokorny-Lehrer, B., Legg, M.S.G, Brade, L., Brade, H., Kosma, P. & Evans, S.V. (2022) Antigen binding by conformational selection in near-germline antibodies. J. Biol. Chem. 298, 101901.

Legg, M.S.G, Hager-Mair, F.F, Krauter, S., Gagnon, S.M.L, Lòpez-Guzmán, A., Lim, C., Blaukopf, M., Kosma, P., Schäffer, C. & Evans, S.V. (2022) The S-layer homology domains of Paenibacillus alvei surface protein SpaA bind to cell wall polysaccharide through the terminal monosaccharide residue. J Biol Chem. 298, 101745.

Haji-Ghassemi, O., Müller-Loennies, S.V., Brooks, C.L., Caveney, N., MacKenzie, C.R., Van Petegem, F., Brade, L., Kosma, P., Brade, H. & Evans, S.V. (2019) A Single Arginine to Lysine Mutation in mAb S25-23 Increases Antibody-Carbohydrate Binding Affinity by an Order of Magnitude.  Biochemistry, 58(6), 714-726.

Gagnon, S.M.L., Legg, M.S.G., Polakowski, R., Letts, J.A., Persson, M., Lin, S., Zheng, R.B., Rempel, B., Schuman, B., Haji-Ghassemi, O., Borisova, S.N., Palcic, M.M. & Evans, S.V. (2018) Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases, Glycobiology 28, 624-636.

Blackler, R.J., López-Guzmán, A., Martinz, G., Gagnon, S.M.L., Haji-Ghassemi, O., Kosma, P., Messner, P., Schäffer, C. & Evans, S.V. (2018) Surface-layer homology domains of Paenibacillus alvei SpaA possess mutually-exclusive binding sites for dynamic cell surface anchoring, Nature Communications, 9, Article number: 3120.

Gagnon, S.M.L.†, Legg, M.S.G.†, Sindhuwinata, N.†, Letts, J.A., Johal, A.R., Schuman, B., Borisova, S.N., Palcic, M.M., Peters, P. & Evans, S.V. (2017) High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggests a molecular basis for product release, Glycobiology, 27, 966-977.

Blackler, R.J., Gagnon, S.M.L., Polakowski, R., Rose, N.L., Zheng, R.B., Letts, J.A., Johal, A.R., Schuman, B., Borisova, S.N., Palcic, M.M. & Evans, S.V. (2017) Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site, Glycobiology, 27, 370-380.

Haji-Ghassemi, O., Gilbert, M., Spence, J., Schur, M.J., Parker, M.J., Jenkins, M.L., Burke, J.E., van Faassen, H., Young, N.M., Evans S.V. (2016) Molecular Basis for Recognition of the Cancer Glycobiomarker, LacdiNAc (GalNAc[β1→4]GlcNAc) by Wisteria floribunda Agglutinin. J. Biol. Chem. 291(46), 24085-24095.

Haji-Ghassemi, O., Müller-Loennies, S., Rodriguez, T., Brade, L., Grimmecke. H.-D., Brade, H. & Evans, S.V. (2016) The Combining Sites of Anti-Lipid A Antibodies Reveal a Widely-Utilized Motif Specific for Negatively Charged Groups.  J. Biol. Chem. 291(19), 10104-10118.

Blackler, R.J., Evans, D.W., Smith, D.F., Brooks, C.L., Braulke, T., Liu, X., Evans, S.V.† & Müller-Loennies, S.† (2016) Single-chain antibody-fragment M6P-1 possesses a mannose 6-phosphate monosaccharide-specific binding pocket that distinguishes N-glycan phosphorylation in a branch-specific manner, Glycobiology, 26(2), 181-192