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  • Journal article
    York WS, Mazumder R, Ranzinger R, Edwards N, Kahsay R, Aoki-Kinoshita KF, Campbell MP, Cummings RD, Feizi T, Martin M, Natale DA, Packer NH, Woods RJ, Agarwal G, Arpinar S, Bhat S, Blake J, Castro LJG, Fochtman B, Gildersleeve J, Goldman R, Holmes X, Jain V, Kulkarni S, Mahadik R, Mehta A, Mousavi R, Nakarakommula S, Navelkar R, Pattabiraman N, Pierce MJ, Ross K, Vasudev P, Vora J, Williamson T, Zhang Wet al., 2020,

    GlyGen: Computational and Informatics Resources for Glycoscience

    , GLYCOBIOLOGY, Vol: 30, Pages: 72-73, ISSN: 0959-6658
  • Journal article
    Azevedo HS, Braunschweig AB, Chiechi RC, Claridge SA, Cronin L, Diaz Fernandez Y, Feizi T, Hartmann L, Huang M, Miura Y, Palma M, Qiu X, Ravoo BJ, Schmidt S, Turnbull WB, Werner C, Zheng Z, Zhou Det al., 2019,

    New directions in surface functionalization and characterization: general discussion.

    , Faraday Discuss, Vol: 219, Pages: 252-261
  • Journal article
    Ten F, 2019,

    Nanolithography of biointerfaces

    , FARADAY DISCUSSIONS, Vol: 219, Pages: 262-275, ISSN: 1359-6640
  • Journal article
    Wu N, Silva LM, Liu Y, Zhang Y, Gao C, Zhang F, Fu L, Peng Y, Linhardt R, Kawasaki T, Mulloy B, Chai W, Feizi Tet al., 2019,

    Glycan Markers of Human Stem Cells Assigned with Beam Search Arrays.

    , Mol Cell Proteomics, Vol: 18, Pages: 1981-2002, ISSN: 1535-9476

    Glycan antigens recognized by monoclonal antibodies have served as stem cell markers. To understand regulation of their biosynthesis and their roles in stem cell behavior precise assignments are required. We have applied state-of-the-art glycan array technologies to compare the glycans bound by five antibodies that recognize carbohydrates on human stem cells. These are: FC10.2, TRA-1-60, TRA-1-81, anti-i and R-10G. Microarray analyses with a panel of sequence-defined glycans corroborate that FC10.2, TRA-1-60, TRA-1-81 recognize the type 1-(Galβ-3GlcNAc)-terminating backbone sequence, Galβ-3GlcNAcβ-3Galβ-4GlcNAcβ-3Galβ-4GlcNAc, and anti-i, the type 2-(Galβ-4GlcNAc) analog, Galβ-4GlcNAcβ-3Galβ-4GlcNAcβ-3Galβ-4GlcNAc, and we determine substituents they can accommodate. They differ from R-10G, which requires sulfate. By Beam Search approach, starting with an antigen-positive keratan sulfate polysaccharide, followed by targeted iterative microarray analyses of glycan populations released with keratanases and mass spectrometric monitoring, R-10G is assigned as a mono-sulfated type 2 chain with 6-sulfation at the penultimate N-acetylglucosamine, Galβ-4GlcNAc(6S)β-3Galβ-4GlcNAcβ-3Galβ-4GlcNAc. Microarray analyses using newly synthesized glycans corroborate the assignment of this unique determinant raising questions regarding involvement as a ligand in the stem cell niche.
  • Journal article
    Wells L, Feizi T, 2019,

    Editorial overview: Carbohydrates: O-glycosylation

    , CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 56, Pages: III-V, ISSN: 0959-440X
  • Journal article
    Chandra N, Liu Y, Liu J-X, Fraengsmyr L, Wu N, Silva LM, Lindstrom M, Chai W, Domellof FP, Feizi T, Arnberg Net al., 2019,

    Sulfated glycosaminoglycans as viral decoy receptors for human adenovirus type 37

    , Viruses, Vol: 11, ISSN: 1999-4915

    Glycans on plasma membranes and in secretions play important roles in infection by many viruses. Species D human adenovirus type 37 (HAdV-D37) is a major cause of epidemic keratoconjunctivitis (EKC) and infects target cells by interacting with sialic acid (SA)-containing glycans via the fiber knob domain of the viral fiber protein. HAdV-D37 also interacts with sulfated glycosaminoglycans (GAGs), but the outcome of this interaction remains unknown. Here, we investigated the molecular requirements of HAdV-D37 fiber knob:GAG interactions using a GAG microarray and demonstrated that fiber knob interacts with a broad range of sulfated GAGs. These interactions were corroborated in cell-based assays and by surface plasmon resonance analysis. Removal of heparan sulfate (HS) and sulfate groups from human corneal epithelial (HCE) cells by heparinase III and sodium chlorate treatments, respectively, reduced HAdV-D37 binding to cells. Remarkably, removal of HS by heparinase III enhanced the virus infection. Our results suggest that interaction of HAdV-D37 with sulfated GAGs in secretions and on plasma membranes prevents/delays the virus binding to SA-containing receptors and inhibits subsequent infection. We also found abundant HS in the basement membrane of the human corneal epithelium, which may act as a barrier to sub-epithelial infection. Collectively, our findings provide novel insights into the role of GAGs as viral decoy receptors and highlight the therapeutic potential of GAGs and/or GAG-mimetics in HAdV-D37 infection.
  • Journal article
    Rudkin FM, Raziunaite I, Workman H, Essono S, Belmonte R, MacCallum DM, Johnson EM, Silva L, Palma AS, Feizi T, Jensen A, Erwig LP, Gow NARet al., 2019,

    Single human B cell-derived monoclonal anti-Candida antibodies enhance phagocytosis and protect against disseminated candidiasis (vol 9, 5288, 2018)

    , NATURE COMMUNICATIONS, Vol: 10, ISSN: 2041-1723
  • Journal article
    Rudkin FM, Raziunaite I, Workman H, Essono S, Belmonte R, MacCallum DM, Johnson EM, Silva LM, Palma AS, Feizi T, Jensen A, Erwig LP, Gow NARet al., 2018,

    Single human B cell-derived monoclonal anti-Candida antibodies enhance phagocytosis and protect against disseminated candidiasis

    , NATURE COMMUNICATIONS, Vol: 9, ISSN: 2041-1723
  • Conference paper
    Akune Y, Arpinar S, Silva LM, Stoll M, Palma AS, Liu Y, Ranzinger R, Feizi Tet al., 2018,

    CarbArrayART: Carbohydrate Array Analysis and Reporting Tool New software for glycan array for data processing, storage and presentation

    , Annual Meeting of the Society-for-Glycobiology (SFG), Publisher: OXFORD UNIV PRESS INC, Pages: 1034-1035, ISSN: 0959-6658
  • Journal article
    Li Z, Feizi T, 2018,

    The neoglycolipid (NGL) technology-based microarrays and future prospects.

    , FEBS Lett, Vol: 592, Pages: 3976-3991

    The neoglycolipid (NGL) technology is the basis of a state-of-the-art oligosaccharide microarray system, which we offer for screening analyses to the broad scientific community. We review here the sequential development of the technology and its power in pinpointing and isolating naturally occurring ligands for glycan-binding proteins (GBPs) within glycan populations. We highlight our Designer Array approach and Beam Search Array approach for generating natural glycome arrays to identify novel ligands of biological relevance. These two microarray approaches have been applied for assignments of ligands or antigens on glucan polysaccharides for effector proteins of the immune system (Dectin-1, DC-SIGN and DC-SIGNR) and carbohydrate-binding modules (CBMs) on bacterial hydrolases. We also discuss here the more recent applications to elucidate the structure of a prostate cancer- associated antigen F77 and identify ligands for adhesins of two rotaviruses, P[10] and P[19], expressed on an epithelial mucin glycoprotein.

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