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• Journal article
  Lenman A, Liaci AM, Liu Y, Ardahl C, Rajan A, Nilsson E, Bradford W, Kaeshammer L, Jones MS, Frangsmyr L, Feizi T, Stehle T, Arnberg Net al., 2015,

  Human Adenovirus 52 Uses Sialic Acid-containing Glycoproteins and the Coxsackie and Adenovirus Receptor for Binding to Target Cells

  , PLOS PATHOGENS, Vol: 11, ISSN: 1553-7366
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  • Citations: 48
• Conference paper
  Liu Y, Catera R, Krammer F, Gao C, Yan X-J, Rai KR, Barrientos JC, Allen SL, Kolitz JE, Garcia-Sastre A, Feizi T, Chiorazzi Net al., 2014,

  IGHV4-34 B-Cell Receptor Immunoglobulins from CLL Stereotyped Subset 4 React with Influenza A Virus: Requirement for IGHV-D-J/Iglv-J Rearrangement and Isotype Switching to IgG

  , 56th Annual Meeting of the American-Society-of-Hematology, Publisher: AMER SOC HEMATOLOGY, ISSN: 0006-4971
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• Conference paper
  Hanashima S, Kanagawa M, Goetze S, Liu Y, Ikeda A, Silva DV, Feizi T, Seeberger P, Yamaguchi Yet al., 2014,

  NMR interaction analysis of intestinal soluble lectin ZG16p with mycobacterium phosphatidylinositol mannosides

  , Joint Meeting of the Society-for-Glycobiology (SFG) and the Japanese-Society-of-Carbohydrate-Research (JSCR), Publisher: OXFORD UNIV PRESS INC, Pages: 1133-1134, ISSN: 0959-6658
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• Journal article
  Panagos CG, Thomson DS, Moss C, Hughes AD, Kelly MS, Liu Y, Chai W, Venkatasamy R, Spina D, Page CP, Hogwood J, Woods RJ, Mulloy B, Bavington CD, Uhrin Det al., 2014,

  Fucosylated Chondroitin Sulfates from the Body Wall of the Sea Cucumber Holothuria forskali CONFORMATION, SELECTIN BINDING, AND BIOLOGICAL ACTIVITY

  , Journal of Biological Chemistry, Vol: 289, Pages: 28284-28298, ISSN: 0021-9258

  Fucosylated chondroitin sulfate (fCS) extracted from the sea cucumber Holothuria forskali is composed of the following repeating trisaccharide unit: →3)GalNAcβ4,6S(1→4) [FucαX(1→3)]GlcAβ(1→, where X stands for different sulfation patterns of fucose (X = 3,4S (46%), 2,4S (39%), and 4S (15%)). As revealed by NMR and molecular dynamics simulations, the fCS repeating unit adopts a conformation similar to that of the Lex blood group determinant, bringing several sulfate groups into close proximity and creating large negative patches distributed along the helical skeleton of the CS backbone. This may explain the high affinity of fCS oligosaccharides for L- and P-selectins as determined by microarray binding of fCS oligosaccharides prepared by Cu2+-catalyzed Fenton-type and photochemical depolymerization. No binding to E-selectin was observed. fCS poly- and oligosaccharides display low cytotoxicity in vitro, inhibit human neutrophil elastase activity, and inhibit the migration of neutrophils through an endothelial cell layer in vitro. Although the polysaccharide showed some anti-coagulant activity, small oligosaccharide fCS fragments had much reduced anticoagulant properties, with activity mainly via heparin cofactor II. The fCS polysaccharides showed prekallikrein activation comparable with dextran sulfate, whereas the fCS oligosaccharides caused almost no effect. The H. forskali fCS oligosaccharides were also tested in a mouse peritoneal inflammation model, where they caused a reduction in neutrophil infiltration. Overall, the data presented support the action of fCS as an inhibitor of selectin interactions, which play vital roles in inflammation and metastasis progression. Future studies of fCS-selectin interaction using fCS fragments or their mimetics may open new avenues for therapeutic intervention.

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• Journal article
  Suits MDL, Pluvinage B, Law A, Liu Y, Palma AS, Chai W, Feizi T, Boraston ABet al., 2014,

  Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of Its hyaluronan-specific carbohydrate-binding module

  , Journal of Biological Chemistry, Vol: 289, Pages: 27264-27277, ISSN: 0021-9258

  For a subset of pathogenic microorganisms, including Streptococcus pneumoniae, the recognition and degradation of host hyaluronan contributes to bacterial spreading through the extracellular matrix and enhancing access to host cell surfaces. The hyaluronate lyase (Hyl) presented on the surface of S. pneumoniae performs this role. Using glycan microarray screening, affinity electrophoresis, and isothermal titration calorimetry we show that the N-terminal module of Hyl is a hyaluronan-specific carbohydrate-binding module (CBM) and the founding member of CBM family 70. The 1.2 Å resolution x-ray crystal structure of CBM70 revealed it to have a β-sandwich fold, similar to other CBMs. The electrostatic properties of the binding site, which was identified by site-directed mutagenesis, are distinct from other CBMs and complementary to its acidic ligand, hyaluronan. Dynamic light scattering and solution small angle x-ray scattering revealed the full-length Hyl protein to exist as a monomer/dimer mixture in solution. Through a detailed analysis of the small angle x-ray scattering data, we report the pseudoatomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl.

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• Book chapter
  Liu Y, Childs RA, Feizi T, 2014,

  Neoglycolipid (NGL)-Based Glycan Microarray System for Ligand Discovery

  , Glycoscience: Biology and Medicine, Editors: Endo, Seeberger, Hart, Wong, Taniguchi, Publisher: Springer Japan, ISBN: 978-4-431-54836-2

  It is now appreciated that carbohydrate–protein interactions are integral to many physiological processes and are directly or indirectly involved in the majority of disease processes, infective or noninfective, including cancer. Carbohydrate microarrays have emerged as powerful tools for elucidating the ligands involved in these interactions. However, as oligosaccharides cannot be cloned and expressed as with DNA and proteins, few laboratories have libraries of sequence-defined oligosaccharide probes with sufficient breadth to tackle the unraveling of diverse carbohydrate–protein interactions. Microarray screening analyses are offered to the scientific community by the Wellcome Trust-supported carbohydrate microarray facility in the Glycosciences Laboratory at Imperial College London and by the NIH-supported Consortium for Functional Glycomics. This chapter gives a brief account of a technology, the neoglycolipid (NGL) technology, first introduced in 1985 and converted into a glycan microarray system in 2002. Results are highlighted from analyses using this system, also including designer arrays, which entail microarrays of NGLs specifically derived from relevant ligand-bearing glycomes in order to reveal the oligosaccharide ligands they harbor and lead to their isolation and characterization. These include discoveries of new ligands in endogenous recognition and pathogen–host interactions and assignments of long-sought cancer-associated antigens.

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• Journal article
  Kanagawa M, Liu Y, Hanashima S, Ikeda A, Chai W, Nakano Y, Kojima-Aikawa K, Feizi T, Yamaguchi Yet al., 2014,

  Structural Basis for Multiple Sugar Recognition of Jacalin-related Human ZG16p Lectin

  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 289, Pages: 16954-16965
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  • Citations: 28
• Journal article
  Gao C, Liu Y, Zhang H, Zhang Y, Fukuda MN, Palma AS, Kozak RP, Childs RA, Nonaka M, Li Z, Siegel DL, Hanfland P, Peehl DM, Chai W, Greene MI, Ten Fet al., 2014,

  Carbohydrate Sequence of the Prostate Cancer-associated Antigen F77 Assigned by a Mucin <i>O</i>-Glycome Designer Array

  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 289, Pages: 16462-16477, ISSN: 0021-9258
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  • Citations: 37
• Journal article
  Nonaka M, Fukuda MN, Gao C, Li Z, Zhang H, Greene MI, Peehl DM, Ten F, Fukuda Met al., 2014,

  Determination of Carbohydrate Structure Recognized by Prostate-specific F77 Monoclonal Antibody through Expression Analysis of Glycosyltransferase Genes

  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 289, Pages: 16478-16486
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  • Citations: 26
• Journal article
  Khan ZM, Liu Y, Neu U, Gilbert M, Ehlers B, Feizi T, Stehle Tet al., 2014,

  Crystallographic and Glycan Microarray Analysis of Human Polyomavirus 9 VP1 Identifies <i>N</i>-Glycolyl Neuraminic Acid as a Receptor Candidate

  , JOURNAL OF VIROLOGY, Vol: 88, Pages: 6100-6111, ISSN: 0022-538X
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  • Citations: 30

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