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  • Conference paper
    Stappers MHT, Clark AE, Aimanianda V, Bidula S, Reid DM, Asamaphan P, Hardison SE, Dambuza IM, Valsecchi I, Kerscher B, Plato A, Wallace CA, Yuecel R, Hebecker B, Sousa MDGT, Cunha C, Liu Y, Feizi T, Brakhage AA, Kwon-Chung KJ, Gow NAR, Zanda M, Piras M, Zanato C, Jaeger M, Netea MG, Van de Veerdonk FL, Lacerda JF, Campos A, Carvalho A, Willment JA, Latge JP, Brown GDet al., 2018,

    Recognition of DHN-melanin by the C-type lectin, MelLec, is required for protective immunity to Aspergillus fumigatus

    , Publisher: OXFORD UNIV PRESS, Pages: S156-S156, ISSN: 1369-3786
  • Journal article
    Chai W, Zhang Y, Mauri L, Ciampa MG, Mulloy B, Sonnino S, Feizi Tet al., 2018,

    Assignment by Negative-Ion Electrospray Tandem Mass Spectrometry of the Tetrasaccharide Backbones of Monosialylated Glycans Released from Bovine Brain Gangliosides

    , JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, Vol: 29, Pages: 1308-1318, ISSN: 1044-0305

    Gangliosides, as plasma membrane-associated sialylated glycolipids, are antigenic structures and they serve as ligands for adhesion proteins of pathogens, for toxins of bacteria, and for endogenous proteins of the host. The detectability by carbohydrate-binding proteins of glycan antigens and ligands on glycolipids can be influenced by the differing lipid moieties. To investigate glycan sequences of gangliosides as recognition structures, we have underway a program of work to develop a “gangliome” microarray consisting of isolated natural gangliosides and neoglycolipids (NGLs) derived from glycans released from them, and each linked to the same lipid molecule for arraying and comparative microarray binding analyses. Here, in the first phase of our studies, we describe a strategy for high-sensitivity assignment of the tetrasaccharide backbones and application to identification of eight of monosialylated glycans released from bovine brain gangliosides. This approach is based on negative-ion electrospray mass spectrometry with collision-induced dissociation (ESI-CID-MS/MS) of the desialylated glycans. Using this strategy, we have the data on backbone regions of four minor components among the monosialo-ganglioside-derived glycans; these are of the ganglio-, lacto-, and neolacto-series.
  • Journal article
    Lenman A, Liaci AM, Liu Y, Frangsmyr L, Frank M, Blaum BS, Chai W, Podgorski II, Harrach B, Benko M, Feizi T, Stehle T, Arnberg Net al., 2018,

    Polysialic acid is a cellular receptor for human adenovirus 52

    , Proceedings of the National Academy of Sciences of the United States of America, Vol: 115, Pages: E4264-E4273, ISSN: 0027-8424

    Human adenovirus 52 (HAdV-52) is one of only three known HAdVs equipped with both a long and a short fiber protein. While the long fiber binds to the coxsackie and adenovirus receptor, the function of the short fiber in the virus life cycle is poorly understood. Here, we show, by glycan microarray analysis and cellular studies, that the short fiber knob (SFK) of HAdV-52 recognizes long chains of α-2,8-linked polysialic acid (polySia), a large posttranslational modification of selected carrier proteins, and that HAdV-52 can use polySia as a receptor on target cells. X-ray crystallography, NMR, molecular dynamics simulation, and structure-guided mutagenesis of the SFK reveal that the nonreducing, terminal sialic acid of polySia engages the protein with direct contacts, and that specificity for polySia is achieved through subtle, transient electrostatic interactions with additional sialic acid residues. In this study, we present a previously unrecognized role for polySia as a cellular receptor for a human viral pathogen. Our detailed analysis of the determinants of specificity for this interaction has general implications for protein–carbohydrate interactions, particularly concerning highly charged glycan structures, and provides interesting dimensions on the biology and evolution of members of Human mastadenovirus G.
  • Journal article
    Stappers MHT, Clark AE, Aimanianda V, Bidula S, Reid DM, Asamaphan P, Hardison SE, Dambuza IM, Valsecchi I, Kerscher B, Plato A, Wallace CA, Yuecel R, Hebecker B, Teixeira Sousa MDG, Cunha C, Liu Y, Feizi T, Brakhage AA, Kwon-Chung KJ, Gow NAR, Zanda M, Piras M, Zanato C, Jaeger M, Netea MG, de Veerdonk FLV, Lacerda JF, Campos A, Carvalho A, Willment JA, Latge J-P, Brown GDet al., 2018,

    Recognition of DHN-melanin by a C-type lectin receptor is required for immunity to Aspergillus

    , NATURE, Vol: 555, Pages: 382-386, ISSN: 0028-0836

    Resistance to infection is critically dependent on the ability of pattern recognition receptors to recognize microbial invasion and induce protective immune responses. One such family of receptors are the C-type lectins, which are central to antifungal immunity1. These receptors activate key effector mechanisms upon recognition of conserved fungal cell-wall carbohydrates. However, several other immunologically active fungal ligands have been described; these include melanin2,3, for which the mechanism of recognition is hitherto undefined. Here we identify a C-type lectin receptor, melanin-sensing C-type lectin receptor (MelLec), that has an essential role in antifungal immunity through recognition of the naphthalene-diol unit of 1,8-dihydroxynaphthalene (DHN)-melanin. MelLec recognizes melanin in conidial spores of Aspergillus fumigatus as well as in other DHN-melanized fungi. MelLec is ubiquitously expressed by CD31+ endothelial cells in mice, and is also expressed by a sub-population of these cells that co-express epithelial cell adhesion molecule and are detected only in the lung and the liver. In mouse models, MelLec was required for protection against disseminated infection with A. fumigatus. In humans, MelLec is also expressed by myeloid cells, and we identified a single nucleotide polymorphism of this receptor that negatively affected myeloid inflammatory responses and significantly increased the susceptibility of stem-cell transplant recipients to disseminated Aspergillus infections. MelLec therefore recognizes an immunologically active component commonly found on fungi and has an essential role in protective antifungal immunity in both mice and humans.
  • Book chapter
    Liu Y, Palma AS, Ten F, Chai Wet al., 2018,

    Insights Into Glucan Polysaccharide Recognition Using Glucooligosaccharide Microarrays With Oxime-Linked Neoglycolipid Probes

    , CHEMICAL GLYCOBIOLOGY, PT B: MONITORING GLYCANS AND THEIR INTERACTIONS, Editors: Imperiali, Publisher: ELSEVIER ACADEMIC PRESS INC, Pages: 139-167
  • Conference paper
    Liu Y, Catera R, Gao C, Yan J, Magli A, Allen SL, Rai K, Chu CC, Stamatopoulos K, Chiorazzi N, Kolitz JE, Feizi Tet al., 2017,

    The (auto)antigen specificities of B cell receptor immunoglobulins from CLL stereotyped subset 4 are positively and negatively selected by structural elements introduced by somatic mutation and isotype class switching

    , Publisher: TAYLOR & FRANCIS LTD, Pages: 80-81, ISSN: 1042-8194
  • Conference paper
    Akune Y, Arpinar S, Stoll M, Silva LM, Palma AS, Liu Y, Ranzinger R, Feizi Tet al., 2017,

    New software for glycan array for data processing, storage and presentation

    , Annual Meeting of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1204-1204, ISSN: 0959-6658
  • Journal article
    Li Z, Gao C, Zhang Y, Palma A, Childs R, Silva L, Liu Y, Jiang X, Liu Y, Chai W, Feizi Tet al., 2017,

    O-Glycome beam search arrays for carbohydrate ligand discovery

    , Molecular and Cellular Proteomics, Vol: 17, Pages: 121-133, ISSN: 1535-9476

    O-glycosylation is a post-translational modification of proteins crucial to molecular mechanisms in health and disease. O-glycans are typically highly heterogeneous. The involvement of specific O-glycan sequences in many bio-recognition systems is yet to be determined due to a lack of efficient methodologies. We describe here a targeted microarray approach: O-glycome beam search that is both robust and efficient for O-glycan ligand-discovery. Substantial simplification of the complex O-glycome profile and facile chromatographic resolution is achieved by arraying O-glycans as branches, monitoring by mass spectrometry, focusing on promising fractions, and on-array immuno-sequencing. This is orders of magnitude more sensitive than traditional methods. We have applied beam search approach to porcine stomach mucin and identified extremely minor components previously undetected within the O-glycome of this mucin that are ligands for the adhesive proteins of two rotaviruses. The approach is applicable to O-glycome recognition studies in a wide range of biological settings to give insights into glycan recognition structures in natural microenvironments.
  • Conference paper
    Panagos C, Moss C, Bavington C, Mulloy B, Feizi T, Chai W, Woods R, Uhrin Det al., 2017,

    Analysis of the 3D structure of fucosylated chondroitin sulfate from H. forskali and its interaction with selectins

    , 254th National Meeting and Exposition of the American-Chemical-Society (ACS) on Chemistry's Impact on the Global Economy, Publisher: AMER CHEMICAL SOC, ISSN: 0065-7727
  • Journal article
    Catera R, Liu Y, Gao C, Yan X-J, Magli A, Allen SL, Kolitz JE, Rai KR, Chu CC, Feizi T, Stamatopoulos K, Chiorazzi Net al., 2017,

    Binding of CLL Subset 4 B Cell Receptor Immunoglobulins to Viable Human Memory B Lymphocytes Requires a Distinctive IGKV Somatic Mutation

    , MOLECULAR MEDICINE, Vol: 23, Pages: 1-12, ISSN: 1076-1551

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