Irma van Die

ORCID: 0000-0002-1505-0452
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About
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Escherichia coli research studies
  • Galectins and Cancer Biology
  • Carbohydrate Chemistry and Synthesis
  • Bacterial Genetics and Biotechnology
  • RNA and protein synthesis mechanisms
  • Monoclonal and Polyclonal Antibodies Research
  • Bacteriophages and microbial interactions
  • Cell Adhesion Molecules Research
  • Enzyme Production and Characterization
  • Cytomegalovirus and herpesvirus research
  • Polysaccharides and Plant Cell Walls
  • Immunotherapy and Immune Responses
  • Cancer-related gene regulation
  • Enzyme Structure and Function
  • Transgenic Plants and Applications
  • Cancer Research and Treatments
  • Immune Response and Inflammation
  • Immune Cell Function and Interaction
  • Proteoglycans and glycosaminoglycans research
  • RNA Research and Splicing
  • Immune responses and vaccinations
  • Renal Diseases and Glomerulopathies
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Reproductive System and Pregnancy

Amsterdam UMC Location Vrije Universiteit Amsterdam
2009-2022

Vrije Universiteit Amsterdam
1998-2022

Amsterdam University Medical Centers
2020

Amsterdam Neuroscience
2015-2016

University of Oklahoma
2004

Protein Express (United States)
2004

Sidney Kimmel Cancer Center
2004

Scripps Research Institute
2004

Tokyo Metropolitan Institute of Gerontology
1998

Johns Hopkins University
1996

Here we describe a glycan microarray constructed by using standard robotic printing technology to couple amine functionalized glycans an amino-reactive glass slide. The array comprises 200 synthetic and natural sequences representing major structures of glycoproteins glycolipids. has remarkable utility for profiling the specificity diverse range binding proteins, including C-type lectins, siglecs, galectins, anticarbohydrate antibodies, lectins from plants microbes, intact viruses.

10.1073/pnas.0407902101 article EN Proceedings of the National Academy of Sciences 2004-11-24

The dendritic cell specific C‐type lectin ICAM‐3 grabbing non‐integrin (DC‐SIGN) binds to “self” glycan ligands found on human cells and “foreign” glycans of bacterial or parasitic pathogens. Here, we investigated the binding properties DC‐SIGN a large array potential in format. Our data indicate that with K d < 2 μM neoglycoconjugate which Galβ1‐4(Fucα1‐3)GlcNAc (Le x ) trisaccharides are expressed multivalently. A lower selective was observed oligomannose‐type N ‐glycans, diantennary...

10.1016/j.febslet.2006.10.009 article EN FEBS Letters 2006-10-16

P-selectin glycoprotein ligand-1 (PSGL-1) is a dimeric membrane mucin on leukocytes that binds selectins. The molecular features of PSGL-1 determine this high affinity binding are unclear. Here we demonstrate the <i>in vitro</i> synthesis novel glycosulfopeptide (GSP-6) modeled after extreme N terminus PSGL-1, which has been predicted to be important for binding. GSP-6 contains three tyrosine sulfate (TyrSO<sub>3</sub>) residues and monosialylated, core 2-based <i>O</i>-glycan with sialyl...

10.1074/jbc.274.35.24838 article EN cc-by Journal of Biological Chemistry 1999-08-01

Abstract The spike (S) glycoprotein in the envelope of SARS-CoV-2 is densely glycosylated but functions its glycosylation are unknown. Here we demonstrate that S recognized a glycan-dependent manner by multiple innate immune receptors including mannose receptor MR/CD206, DC-SIGN/CD209, L-SIGN/CD209L, and MGL/CLEC10A/CD301. Single-cell RNA sequencing analyses indicate such highly expressed cells tissues susceptible to infection. Binding above characterized affinities picomolar range...

10.1101/2020.07.29.227462 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-07-30

Abstract Sialoadhesin (Siglec-1) is a macrophage-restricted sialic acid-binding receptor that mediates interactions with hemopoietic cells, including lymphocytes. In this study, we identify sialoadhesin counterreceptors on T Several major glycoproteins (85, 130, 240 kDa) were precipitated by sialoadhesin-Fc fusion proteins from murine cell line (TK-1). Binding of to these was acid dependent and abolished mutation critical residue (R97A) the binding site in membrane distal Ig-like domain...

10.4049/jimmunol.166.6.3637 article EN The Journal of Immunology 2001-03-15

Altered glycosylation in epithelial cancers may play an important role tumour progression, as it affect cell migration and antigen presentation by presenting cells. We specifically characterise the patterns of two antigens that are highly expressed cancer tissue often detected their secreted form serum: mucin MUC1 carcinoembryonic (CEA, also called CEACAM5). analysed 48 colorectal patients, comparing normal colon epithelium within each patient. Lectin binding was studied a standardised...

10.1002/ijc.26354 article EN International Journal of Cancer 2011-08-05

Synthesis of parasite specific IgE plays a critical role in the defence against helminth infections. We report here that from serum Schistosoma mansoni infected mice and Haemonchus contortus sheep recognizes complex‐type N‐glycans Arabidopsis thaliana , which contain R‐GlcNAcβ1→4(Fucα1→3)GlcNAcβ1‐Asn (core α1→3‐Fuc) Xylβ1→2Manβ1→4GlcNAcβ1‐R β1→2‐Xyl) modifications, honeybee phospholipase A2, carries core α1→3‐Fuc epitope. Evidence is presented α1→3‐fucosylated bind substantial part H. sheep....

10.1016/s0014-5793(99)01508-2 article EN FEBS Letters 1999-12-07

A cDNA encoding a β-1,4-galactosyltransferase named β-1,4-GalT II was cloned from library of the human breast tumor cell line, MRK-nu-1. Initially, 860-bp PCR fragment obtained MRK-nu-1 mRNA by 3′-rapid amplification ends using two nested degenerate oligonucleotide primers based on highly conserved amino acid sequence found in catalytic domain mammalian β-1,4-galactosyltransferases and Lymnaea stagnalis β-1,4- N -acetylglucosaminyltransferase (β-1,4-GlcNAcT), both which utilize same sugar...

10.1073/pnas.95.2.472 article EN Proceedings of the National Academy of Sciences 1998-01-20

ABSTRACT F1C fimbriae are correlated with uropathogenic Escherichia coli strains. Although mediate binding to kidney tubular cells, their receptor is not known. In this paper, we demonstrate for the first time specific carbohydrate residues as structure F1C-fimbria-expressing E. . The of fimbriated recombinant strain HB101(pPIL110-54) and purified reference glycolipids different compositions was evaluated by using thin-layer chromatography (TLC) overlay solid-phase assays. TLC fimbrial...

10.1128/iai.68.6.3541-3547.2000 article EN Infection and Immunity 2000-06-01

A considerable amount (approximately 1.6 μg from 1 mg of dried nematode) non‐sulfated chondroitin, two orders magnitude less yet an appreciable heparan sulfate, and no hyaluronate were found in Caenorhabditis elegans nematodes. The chondroitin chains heterogeneous size, being shorter than that whale cartilage sulfate. disaccharide composition analysis sulfate revealed diverse sulfation including glucosamine 2‐ N ‐sulfation, 6‐ O ‐sulfation uronate ‐sulfation. These results imply are involved...

10.1016/s0014-5793(99)01286-7 article EN FEBS Letters 1999-10-12

The dendritic cell-specific C-type lectin DC-SIGN functions as a pathogen receptor that recognizes Schistosoma mansoni egg antigens through its major glycan epitope Galbeta1,4(Fucalpha1,3)GlcNAc (Lex). Here we report L-SIGN, highly related homologue of found on liver sinusoidal endothelial cells, binds to S. but not the Lex epitope. L-SIGN does bind Lewis Lea, Leb, and Ley, similar DC-SIGN. A specific mutation in carbohydrate recognition domain (V351G) abrogates binding all antigens. In...

10.1074/jbc.m404988200 article EN cc-by Journal of Biological Chemistry 2004-06-08

Cosmc is the specific molecular chaperone in endoplasmic reticulum for T-synthase, a Golgi β3-galactosyltransferase that generates core 1 O-glycan, Galβ1–3GalNAcα-Ser/Thr, glycoproteins. Dysfunctional results formation of inactive T-synthase and consequent expression Tn antigen (GalNAcα1-Ser/Thr), which associated with several human diseases. However, regulation Cosmc, encoded by single gene on Xq24, poorly understood. Here we show epigenetic silencing through hypermethylation its promoter...

10.1074/jbc.m112.371989 article EN cc-by Journal of Biological Chemistry 2012-10-04

Clinical trials have shown that administration of the nematode Trichuris suis can be beneficial in treating various immune disorders. To provide insight into mechanisms by which this worm suppresses inflammatory responses, an active component was purified from T. soluble products (TsSPs) suppress TNF and IL-12 secretion LPS-activated human dendritic cells (DCs). Analysis liquid chromatography tandem mass spectrometry identified compound as prostaglandin (PG)E2. The showed similar properties...

10.1096/fj.201600841r article EN The FASEB Journal 2016-11-02

We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which bacterium is involved synthesis of lacto-N-neo-tetraose structural element bacterial lipooligosaccharide, was obtained an enzymatically highly active form. This glycosyltransferase appeared be unusual that it displays broad acceptor specificity toward both α- and β-galactosides, whether structurally related N- or O-protein-,...

10.1093/glycob/9.10.1061 article EN Glycobiology 1999-10-01

The choice for a heterologous expression system to produce glycoprotein therapeutics highly depends on its potential perform mammalian-like posttranslational modifications such as glycosylation. To gain more insight into the glycosylation of baculovirus mediated insect cell system, we have studied glycosyltransferases involved in complex-type N-glycosylation. Lepidopteran lines derived from Trichoplusia ni, Spodoptera frugiperda, and Mamestra brassicae were found express beta 1-->4-...

10.1093/glycob/6.2.157 article EN Glycobiology 1996-01-01

Fimbrial adhesins enable bacteria to attach eucaryotic cells. The genetic determinants for S fimbrial (sfa) and F1C ("pseudotype I") fimbriae (foc) were compared. Sfa represent functionally distinct in their receptor specificities. Nevertheless, a high degree of homology between both was found on the basis DNA-DNA hybridizations. Characteristic differences restriction maps corresponding gene clusters, however, visible regions coding subunits S-specific adhesin. While plasmid carrying...

10.1128/jb.170.9.3983-3990.1988 article EN Journal of Bacteriology 1988-09-01

Abstract The endothelium plays a central role in the logistics of immune system by allowing selective transmigration leukocytes, as well maintenance circulation and coagulation homeostasis. Evidence is increasing that carbohydrate composition endothelial cell surface critical for cells to exert their physiological function. major aim this study unravel mechanisms underlying expression structures cells, which are involved leukocyte adhesion migration. Using quantitative real‐time PCR, profile...

10.1002/jcp.20458 article EN Journal of Cellular Physiology 2005-08-03

A common terminal structure in glycans from animal glycoproteins and glycolipids is the lactosamine sequence Galβ4GlcNAc-R (LacNAc or LN). An alternative that occurs vertebrate as well invertebrate glycoconjugates GalNAcβ4GlcNAc-R (LacdiNAc LDN). Whereas genes encoding β4GalTs responsible for LN synthesis have been reported, β4GalNAcT(s) LDN has not identified. Here we report identification of a gene fromCaenorhabditis elegans UDP-GalNAc:GlcNAcβ-R β1,4-N-acetylgalactosaminyltransferase...

10.1074/jbc.m206112200 article EN cc-by Journal of Biological Chemistry 2002-09-01

The genetic organization of the foc gene cluster has been studied; six genes involved in biogenesis F1C fimbriae were identified. focA encodes major fimbrial subunit, focC a product that is indispensable for fimbria formation, focG and focH encode minor subunits, focI protein which shows similarities to subunit FocA. Apart from FocA purified contain at least two FocG FocH. Minor proteins similar size observed S fimbriae. Remarkably, some mutations result an altered morphology, i.e., rigid...

10.1128/jb.172.2.1114-1120.1990 article EN Journal of Bacteriology 1990-02-01
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