LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition

Timo K. Van Den Berg, Henk Honing, Niels Franke, Alexandra Van Remoortere, Wietske E C M Schiphorst, Fu-Tong Liu, André M. Deelder, Richard D. Cummings, Cornells H. Hokke, Irma Van Die

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Abstract

Although Galβ1-4GlcNAc (LacNAc) moieties are the most common constituents of N-linked glycans on vertebrate proteins, GalNAcβ1-4GlcNAc (LacdiNAc, LDN)-containing glycans are widespread in invertebrates, such as helminths. We postulated that LDN might be a molecular pattern for recognition of helminth parasites by the immune system. Using LDN-based affinity chromatography and mass spectrometry, we have identified galectin-3 as the major LDN-binding protein in macrophages. By contrast, LDN binding was not observed with galectin-1. Surface plasmon resonance (SPR) analysis and a solid phase binding assay demonstrated that galectin-3 binds directly to neoglycoconjagates carrying LDN glycans. In addition, galectin-3 bound to Schistosoma mansoni soluble egg Ags and a mAb against the LDN glycan inhibited this binding, suggesting that LDN glycans within S. mansoni soluble egg Ags contribute to galectin-3 binding. Immunocytochemistry demonstrated high levels of galectin-3 in liver granulomas of S. mansoni-infected hamsters, and a colocalization of galectin-3 and LDN glycans was observed on the parasite eggshells. Finally, we demonstrate that galectin-3 can mediate recognition and phagocytosis of LBN-coated particles by macrophages. These findings provide evidence that LDN-glycans constitute a parasite pattern for galectin-3-mediated immune recognition.

Original languageEnglish (US)
Pages (from-to)1902-1907
Number of pages6
JournalJournal of Immunology
Volume173
Issue number3
StatePublished - Aug 1 2004

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Galectin 3
Polysaccharides
Parasites
Schistosoma mansoni
Helminths
Ovum
Macrophages
N-acetylgalactosaminyl-1-4-N-acetylglucosamine
Galectin 1
Egg Shell
Surface Plasmon Resonance
Invertebrates
Granuloma
Affinity Chromatography
Phagocytosis
Cricetinae
Vertebrates
Immune System
Mass Spectrometry
Carrier Proteins

ASJC Scopus subject areas

  • Immunology

Cite this

Van Den Berg, T. K., Honing, H., Franke, N., Van Remoortere, A., Schiphorst, W. E. C. M., Liu, F-T., ... Van Die, I. (2004). LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition. Journal of Immunology, 173(3), 1902-1907.

LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition. / Van Den Berg, Timo K.; Honing, Henk; Franke, Niels; Van Remoortere, Alexandra; Schiphorst, Wietske E C M; Liu, Fu-Tong; Deelder, André M.; Cummings, Richard D.; Hokke, Cornells H.; Van Die, Irma.

In: Journal of Immunology, Vol. 173, No. 3, 01.08.2004, p. 1902-1907.

Research output: Contribution to journalArticle

Van Den Berg, TK, Honing, H, Franke, N, Van Remoortere, A, Schiphorst, WECM, Liu, F-T, Deelder, AM, Cummings, RD, Hokke, CH & Van Die, I 2004, 'LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition', Journal of Immunology, vol. 173, no. 3, pp. 1902-1907.
Van Den Berg TK, Honing H, Franke N, Van Remoortere A, Schiphorst WECM, Liu F-T et al. LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition. Journal of Immunology. 2004 Aug 1;173(3):1902-1907.
Van Den Berg, Timo K. ; Honing, Henk ; Franke, Niels ; Van Remoortere, Alexandra ; Schiphorst, Wietske E C M ; Liu, Fu-Tong ; Deelder, André M. ; Cummings, Richard D. ; Hokke, Cornells H. ; Van Die, Irma. / LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition. In: Journal of Immunology. 2004 ; Vol. 173, No. 3. pp. 1902-1907.
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AU - Schiphorst, Wietske E C M

AU - Liu, Fu-Tong

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