For a complete list of publications, please go to the principal investigator website.

Project: Clostridium difficile

1.      El-Hawiet, A., Kitova, E. N., Kitov, P., Eugenio, L., Ng, K. K. S., Mulvey, G. L., Dingle, T. C., Szpacenko, A., Armstrong, G. D. and Klassen, J. S. Binding of Clostridium difficile Toxins to Human Milk Oligosaccharides. Glycobiology 21, 1217-1227 (2011).

2.      Griener, T. P., Strecker, J., Humphries, R. M., Mulvey, G. L., Fuentealba, C., Hancock, R. E. W. and Armstrong, G. D. Lipopolysaccharide renders transgenic mice expressing human serum amyloid P component sensitive to Shiga toxin 2. PLoS One 6, e21457 (2011).

3.      Mulvey, G. L., Dingle, T. C., Fang, L., Strecker, J. and Armstrong, G. D. Therapeutic potential of egg yolk antibodies for treating Clostridium difficile infection. J. Med. Microbiol. 60, 1181-1187 (2011).

4.      Zhang, P., Razi, N., Eugenio, L., Fentabil, M., Kitova, E. N., Klassen, J. S., Bundle, D. R., Ng, K. K. S. and Ling, C.-C. Unexpected structure of a Clostridium difficile toxin A ligand necessitates an annotation correction in a popular screening library. Chem. Comm. 47, 12397-99 (2011).

5.      Dingle, T., Mulvey, G. L., Humphries, R. M. and Armstrong, G. D. A real-time quantitative PCR assay for evaluating Clostridium difficile adherence to differentiated intestinal Caco-2 cells. J. Med. Microbiol. 59, 920-924 (2010).

6.      Zhang, P., Ng, K. and Ling, C.-C. Efficient synthesis of LeA-LacNAc pentasaccharide as a ligand for Clostridium difficile toxin A. Org. Biomol. Chem. 8, 128-136 (2010).

7.      Dingle, T., Wee, S., Mulvey, G. L., Greco, A., Ng, K., Klassen, J. S. and Armstrong, G. D.. Functional properties of the carboxy-terminal host cell binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile. Glycobiology 18, 698–706 (2008).

Project: Heterobifunctional Ligands

1.      Kitov, P. I., Paszkiewicz, E., Sadowska, J. M., Deng, Z., Ahmed, M., Narain, R., Griener, T., Mulvey, G. L., Armstrong, G. D. and Bundle, D. R. Impact of the nature and size of the polymeric backbone on the ability of heterobifunctional ligands to mediate Shiga toxin and serum amyloid P component ternary complex formation. Toxins 3, 1065-1088 (2011).

2.      Guiard, J., Langpap, B., Kitov, P., Peters, P. and Bundle, D. R. “Double-Click” Protocol for Synthesis of Heterobifunctional Multivalent Ligands: Toward a Focused Library of Specific Norovirus Inhibitors. Chem. Eur. J. 17, 7438-7441 (2011).

3.      Rademacher, C., Guiard, J., Kitov, P., Langpap, B., Dalton, K. P., Parra, F., Bundle, D. R. and Peters, P. Targeting Norovirus Infection – Multivalent Entry Inhibitor based on NMR Data. Chem. Eur. J. 17, 7442-7453 (2011).

4.      Kitov, P. I., Lipinski, T., Paszkiewicz, E., Solomon, D., Sadowska, J. M., Grant, G. G. A., Mulvey, G. L., Kitova, E. N., Klassen, J. S. Armstrong,G. D. and Bundle, D. R.. An entropically efficient supramolecular inhibition strategy for shiga toxins. Angew. Chem. Int. Ed. 47, 672–676 (2008).

5.      O’Reilly, M. K., Collins, B. E., Han, S., Liao, L., Rillahan, C.  Kitov, P. I., Bundle, D. R. and Paulson, J. C. Bi-functional CD22 ligands use multimeric immunoglobulins as protein scaffolds in assembly of immune complexes on B cells. J. Am. Chem. Soc. 130, 7736-7745 (2008).

6.      Kitov, P. I., Mulvey, G. L., Griener, T., Lipinski, T., Solomon, D., Paszkiewicz, E., Jacobson, J., Sadowska, J. M., Suzuki, M., Yamamura, K., Armstrong, G. D. and Bundle, D. R. In vivo supramolecular templating enhances the activity of multivalent ligands: A potential therapeutic against the E. coli O157 AB5 toxins. Proc. Natl. Acad. Sci. ( USA ) 105, 16837-16842 (2008).

7.      Kitova, E. N., Kitov, P. I., Paszkiewicz, E., Kim, J., Mulvey, G. L., Armstrong, G. D., Bundle, D. R. and Klassen, J. S. Affinities of Shiga toxins 1 and 2 for univalent and oligovalent pk trisaccharide analogs measured by electrospray ionization mass spectrometry. Glycobiology 17, 1156-1166 (2007).

Project: Tuberculosis

1.      Murase, T., Zheng, R. B., Joe, M., Bai, Y., Marcus, S. L., Lowary, T. L. and Ng, K. K. S. Structural insights into host recognition of mycobacterial polysaccharides. J. Mol. Biol. 392, 381-392 (2009).

2.      Szczepina, M. G., Zheng, R. B., Completo, G. C., Lowary, T. L., Pinto and B. M. STD-NMR Studies Suggest that Two Acceptor Substrates for GlfT2, a Bifunctional Galactofuranosyltransferase Required for the Biosynthesis of Mycobacterium tuberculosis Arabinogalactan, Compete for the Same Binding Site. ChemBioChem 10, 2052–2059 (2009).

3.      Joe, M., Bai, Y., Nacario, R. C. and Lowary, T. L. Synthesis of the Docosanasaccharide Arabinan Domain of Mycobacterial Arabinogalactan and a Proposed Octadecasaccharide Biosynthetic Precursor. J. Am. Chem. Soc. 129, 9885–9901 (2007).

4.      Rademacher, C., Shoemaker, G. K., Kim, H.-S., Zheng, R. B., Taha, H., Liu, C., Nacario, R. C., Schriemer, D. C., Klassen, J. S., Peters, T. and Lowary, T. L. Ligand Specificity of CS-35, a Monoclonal Antibody that Recognizes Mycobacterial Lipoarabinomannan.  A Model System for Oligofuranoside–Protein Recognition. J. Am. Chem. Soc. 129, 10489–10502 (2007).

5.      Joe, M., Sun, D., Taha, H., Completo, G. C., Croudace, J. E., Lammas, D. A., Besra, G. S. and Lowary, T. L. The 5-Deoxy-5-Methylthio-Xylofuranose Residue in Mycobacterial Lipoarabinomannan.  Absolute Stereochemistry, Linkage Position, Ring Conformation and Immunomodulatory Activity. J. Am. Chem. Soc. 128, 5059–5072 (2006).

6.      Rose, N. L., Completo, G. C., Lin, S.-J., McNeil, M. R., Palcic, M. M. and Lowary, T. L. Expression, Purification and Characterization of a Galactofuranosyl-transferase Involved in Mycobacterium tuberculosis Arabinogalactan Biosynthesis. J. Am. Chem. Soc. 128, 6721–6729 (2006).

Project: Electrospray Ionization Mass Spectrometry

1.      El-Hawiet, A., Shoemaker, G. K., Daneshfar, R., Kitova, E. N. and Klassen J. S. Applications of a Catch and Release Electrospray Ionization Mass Spectrometry Assay for Carbohydrate Library Screening. Anal. Chem. 84, 50–58 (2012).

2.      El-Hawiet, A., Kitova, E. N., Liu, L. and Klassen J. S. Quantifying Labile Protein-Ligand Interactions using Electrospray Ionization Mass Spectrometry. J. Am. Soc. Mass Spectrom. 21, 1893-1899 (2010).

3.      Kitova, E. N., Mulvey, G. L., Dingle, T., Wee, S., Griener, T. P., Armstrong G. D. and Klassen, J.S. Assembly and stability of the Shiga toxins investigated by temperature-controlled electrospray ionization mass spectrometry. Biochemistry 48, 5365-5374 (2009).

4.      Bagal, D., Kitova, E. N., Liu, L., El-Hawiet, A., Schnier, P. D. and Klassen, J. S.. Gas phase Stabilization of noncovalent protein complexes formed by electrospray ionization. Anal Chem. 81, 7801-7806 (2009).

5.      Liu, L., Bagal, D., Kitova, E. N., Schnier, P. D. and Klassen, J. S. Hydrophobic protein-ligand interactions preserved in the gas phase. J. Am. Chem. Soc. 131, 15980-15981 (2009).

6.      Soya, N., Shoemaker, G. K., Palcic, M. M. and Klassen, J. S. Comparative Study of Substrate and Product Binding to the Human ABO(H) Blood Group Glycosyltransferases. Glycobiology 19, 1224-1234 (2009).

Project: Glycoengineering

1.      Hug, I., Zheng, B., Reiz, B., Whittal, R., Fentabil, M. A., Klassen, J. S. and Feldman, M. F. Exploiting bacterial glycosylation machineries for the synthesis of a Lewis antigen-containing glycoprotein. J. Biol. Chem. 286, 37887-37894 (2011).

2.      Ielmini, M. V. and Feldman, M. F. Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. Glycobiology 21, 734-742 (2011).

3.      Nothaft, H. and Szymanski, C. M. Protein glycosylation in bacteria – sweeter than ever. Nat. Rev. Microbiol. 8, 765-778 (2010).

4.      Poulin, M. B., Nothaft, H., Hug, I., Feldman, M., Szymanski, C. M. and Lowary, T. L. Characterization of a bifunctional pyranose-furanose mutase from Campylobacter jejuni 11168. J. Biol. Chem. 285, 493-501 (2010).

5.      Hug, I., Couturier, M. R., Rooker, M. M., Taylor, D. E., Stein, M., Feldman, M. F. Helicobacter pylori lipopolysaccharide is synthesized via a novel pathway with an evolutionary connection to protein N-glycosylation. PLoS Pathog. 6, e1000819 (2010).

6.      Nothaft, H., Liu, X., McNally, D. J., Li, J. and Szymanski, C. M. Study of free oligosaccharides derived from the bacterial N-glycosylation pathway. Proc. Natl. Acad. Sci. ( USA ) 106, 15019-15024 (2009).

7.      Faridmoayer, A., Fentabil, M. A., Haurat, M. F., Yi, W., Woodward, R., Wang, P. G. and Feldman, M.F. Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation. J. Biol. Chem. 283, 34596-34604 (2008).

8.      Faridmoayer, A., Fentabil, M. A., Mills, D. C., Klassen, J. S. and Feldman, M. F. Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation. J. Bacteriol. 189, 8088-8098 (2007).

Project: Exploitation of glycan interactions in the gut

2.      Stahl, M., Friis, L. M., Nothaft, H., Liu, X., Li, J., Szymanski, C. M. and Stintzi, A. L-fucose provides Campylobacter jejuni with a competitive advantage. Proc. Natl. Acad. Sci. ( USA ) 108, 7194-7199 (2011).

3.      Singh, A., Arutyunov, D., McDermott, M. T., Szymanski, C. M. and Evoy, S. Specific detection of Campylobacter jejuni using the bacteriophage NCTC 12673 receptor binding protein as a probe. Analyst 136, 4780-4786 (2011).

4.      Waseh, S., Hanifi-Moghaddam, P., Coleman, R., Masotti, M., Ryan, S., Foss, M., MacKenzie, R., Henry, M, Szymanski, C. M. and Tanha, J. Orally administered P22 phage tailspike protein reduces Salmonella colonization in chickens: prospects of a novel therapy against bacterial infections. PLoS One 5, 1-9 (2010).

5.      Holst-Sørensen, M. C., van Alphen, L. B., Fodor, C., Crowley, S., Bak-Christensen, B., Szymanski, C. M. and Brøndsted, L. Phase variable expression of capsular polysaccharide modifications allows Campylobacter jejuni to avoid bacteriophage infection in chickens. Frontiers Cell. Infect. Microbiol. in-press.

Project: Candida albicans

1.      Bundle, D. R., Costello, C., Nycholat, C., Lipinski, T. and Rennie, R. Designing a Candida albicans Conjugate Vaccine by Reverse Engineering Protective Monoclonal Antibodies in Anticarbohydrate Antibodies: From Molecular Basis to Clinical Application, edited by P. Kosma and S. Muller-Loennies Springer, 121-146, January 2012.

2.      Lipinski, T., Kitov, P., Szpacenko, A., Paszkiewicz, E. and Bundle, D. R. Synthesis and Immunogenicity of a Glycopolymer Conjugate. Bioconjugate Chem. 22, 274–281 (2011).

3.      Xin, H., Dziadek, S., Bundle, D. R. and Cutler, J. Synthetic glycopeptide vaccines combining β-mannan and peptide epitopes induce protection against candidiasis. Proc. Natl. Acad. Sci. ( USA ) 105, 13526-13531 (2008).

Project: Tolerogens

1.      Meloncelli, P. J., West, L. J. and Lowary, T. L.  Synthesis and NMR Studies on the ABO Histo-Blood Group Antigens: Synthesis of Type III and IV Structures and NMR Characterization of Type I–VI Antigens. Carbohydr. Res. 346, 1406–1426 (2011).

2.      Slaney, A. M., Wright, V. A., Meloncelli, P. J., Harris, K. D., West, L. J., Lowary, T. L. and Buriak, J. M. Biocompatible Carbohydrate-Functionalized Stainless Steel Surfaces: A New Method for Passivating Biomedical Implants. ACSApp. Mater. Interfaces 3, 1601–1612 (2011).

3.      Meloncelli, P. J. and Lowary, T. L. Synthesis of ABO Histo-blood Group Type I and II Antigens. Carbohydr. Res. 345, 2304–2321 (2010).

Project: Cyclodextrins

1.      Wang, A., Li, W., Zhang, P. and Ling, C.-C. Synthesis of a Novel Class of Biodegradable Nanotubes. Org. Lett. 13, 3572-3575 (2011).

2.      Ghosh, R., Zhang, P., Wang, A. and Ling, C.-C. Diisobutylaluminum Hydride-Mediated Regioselective O-Desilylations as a Novel Route to Access Multisubstituted Cyclodextrins. Angew. Chem. Int . Ed.  DOI: 10.1002/anie.201105737 (2011).

3.      Ward, S. and Ling, C.-C. Efficient and Versatile Modification of the Secondary Face of Cyclodextrins via Copper-Catalyzed Huisgen 1,3-Dipolar Cycloaddition. Eur. J. Org. Chem. 4853-4861 (2011).

4.      Rawal, G. K., Zhang, P. and Ling, C.-C. Controlled synthesis of linear α-cyclodextrin oligomers using copper-catalyzed Huisgen 1,3-dipolar cycloaddition. Org. Lett. 12, 3096-3099 (2010).

5.      Rawal, G. K., Rani, S., Ward S. and Ling, C.-C. DIBAL-H mediated triple and quadruple debenzylations reactions of perbenzylated cyclodextrins. Org. Biomol. Chem. 8, 171-180 (2010).

Project: Neuraminidase

1.      Albohy, A., Mohan, S., Zheng, R. B., Pinto, B. M. and Cairo, C. W. Inhibitor selectivity of a new class of oseltamivir analogs against viral neuraminidase over human neuraminidase enzymes. Bioorg. Med. Chem. 19, 2817-2822 (2011).

2.      Sandbhor, M. S., Soya, N, Albohy, A., Zheng, R. B., Cartmell, J., Bundle, D. R., Klassen, J. S. and Cairo, C. W. Substrate recognition of the membrane-associated sialidase NEU3 requires a hydrophobic aglycone. Biochemistry 50, 6753-5762 (2011).

3.      Albohy, A., Li, M. D., Zheng, R. B., Zou, C. and Cairo, C.W. Insight into recognition and catalysis of the mammalian neuraminidase 3 (NEU3) through molecular modeling and site directed mutagenesis. Glycobiology 20, 1127-1138 (2010).

4.      Zou, Y., Albohy, A., Sandbhor, M. and Cairo, C. W.  Inhibition of the human neuraminidase 3 (NEU3) by C9-triazole derivatives of 2,3-didehydro-N-acetylneuraminic acid. Bioorg. Med. Chem. Lett. 20, 7529-7533 (2010).

5.      Loka, R. S. and Cairo, C. W. Immobilization of carbohydrate epitopes for surface plasmon resonance using the Staudinger ligation. Carbohydr. Res. 345, 2641-264 (2010).

6.      Loka, R. S., Sadek, C. M., Romaniuk, N. A. and Cairo, C. W. Conjugation of synthetic N-acetyl-lactosamine to azide-containing proteins using the Staudinger ligation. Bioconjugate Chem. 21, 1842-1849 (2010).