Dual Specificity of Langerin to Sulfated and Mannosylated Glycans via a Single C-type Carbohydrate Recognition Domain

Tateno, Hiroaki; Ohnishi, Koji; Yabe, Rikio; Hayatsu, Norihito; Sato, Takashi; Takeya, Motohiro; Narimatsu, Hisashi; Hirabayashi, Jun

doi:10.1074/jbc.m109.041863

Cited by 76 publications

(94 citation statements)

References 44 publications

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“…So far, only a few proteins recognizing a specific modification of a glycan have been described, all of which have endogenous roles: P-type lectin recognizes terminal Man-6-P and has an important role in lysosomal targeting of glycoproteins (44), whereas Langerin binds to Gal-6-SO 4 in sulfated proteoglycans and is involved in the modulation of innate immunity (45). In contrast, fungal Lb-Tec2 is a defense effector protein targeting a specific modification of exogenous glycans.…”

Section: Discussionmentioning

confidence: 99%

Methylated glycans as conserved targets of animal and fungal innate defense

Wohlschlager

Butschi

Grassi

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Effector proteins of innate immune systems recognize specific nonself epitopes. Tectonins are a family of β-propeller lectins conserved from bacteria to mammals that have been shown to bind bacterial lipopolysaccharide (LPS). We present experimental evidence that two Tectonins of fungal and animal origin have a specificity for O-methylated glycans. We show that Tectonin 2 of the mushroom Laccaria bicolor (Lb-Tec2) agglutinates Gram-negative bacteria and exerts toxicity toward the model nematode Caenorhabditis elegans, suggesting a role in fungal defense against bacteria and nematodes. Biochemical and genetic analysis of these interactions revealed that both bacterial agglutination and nematotoxicity of Lb-Tec2 depend on the recognition of methylated glycans, namely O-methylated mannose and fucose residues, as part of bacterial LPS and nematode cell-surface glycans. In addition, a C. elegans gene, termed samt-1, coding for a candidate membrane transport protein for the presumptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi was identified. Intriguingly, limulus lectin L6, a structurally related antibacterial protein of the Japanese horseshoe crab Tachypleus tridentatus, showed properties identical to the mushroom lectin. These results suggest that O-methylated glycans constitute a conserved target of the fungal and animal innate immune system. The broad phylogenetic distribution of O-methylated glycans increases the spectrum of potential antagonists recognized by Tectonins, rendering this conserved protein family a universal defense armor.

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Section: Discussionmentioning

confidence: 99%

Methylated glycans as conserved targets of animal and fungal innate defense

Wohlschlager

Butschi

Grassi

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…Xenopus galectin-VIIa [81] Human, chicken, nematode, sponge, fungal galectrins [36] Human galectin-9 [82] Nematode galectin LEC-1 and N-and C-CRDs [83] C-type PF00059 C-type α/β-fold Atlantic salmon serum [84] calcium-dependent Sea cucumber lectin CEL-IV [85] DC-SIGN, DC-SIGNR, and LSECtin [86] Langerin to sulfated and mannsylated glycans [87] MGL1, MGL2, and their mutants [88] Atlantic salmon C-type lectin receptor C (SCLRC) [89] Acorn barnacle Megabalanus rosa, Balanus rostatus [90] R-type PF00652 β-trefoil Mutants of earthworm lectin EW29Ch [91] ricin B chain-related RCA120/RCA-I [58] Phytopathogenic Sclerotinia sclerotiorum [92] Jacalin-related PF01419 β-prism I Human ZG16 p [93] Mannose-binding type Jacalin-related lectins [37] Jacalin [94] Castanea crenata agglutinin (CCA) [95] Cycas revoluta leaf lectin (CRLL) [95] GNA-related monocot-type PF04152 β-prism II Two-domain GNA-related lectins [96] Sea urchin egg PF02140 α/β-fold with two long Shishamo smelt Osmerus (Spirinchus) lanceolatus [97] Fungal fucose-specific PF07938 6-bladed β-propeller Mushroom Pholiota squarrosa [104] Aspergillus oryzae [105] AAL-like Fungal fruit body lectin PF07367 α/β-sandwich Agaricus bisporus agglutinin (ABA) [106] Others Mussel, Mytilus galloprovincialis [107] orphan or family Mushroom Hygrophorus russula [108] unidentified Eggs of Japanese sea hare Aplysia kurodai [109] Feather star Oxycomanthus japonicas [110] Coronate moon turban Turbo (Lunella)…”

Section: Erythrina Species [58]mentioning

confidence: 99%

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

et al. 2015

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Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms-from humans to microorganisms, including viruses-and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin's function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named "Lectin frontier DataBase (LfDB)", which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (Kd's). For Kd determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. OPEN ACCESS

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“…As regards glycan array, there are several types of platforms on which different types of glycans and glycoconjugates are immobilized: (i) structurally defined synthetic glycans with appropriate spacers [47,48], (ii) natural glycans derived from natural glycoproteins [49,50], (iii) glycopeptides such as those derived from MUC1 [22,24], (iv) fractionated natural glycoproteins [51][52][53], and (v) neoglycoproteins and glycopolymers [54]. These glycan arrays have been used for various purposes, e.g., search for novel glycan-binding proteins [55][56][57], screening for cancer-related autoantibodies [22,24,30,32,[51][52][53], and surveillance of influenza virus [58,59].…”

Section: Emerging Technology Of Lectin Microarraymentioning

confidence: 99%

“…Inclusion of not only plant but also many other lectins from animal, bacteria, and fungi is important to expand the glycome coverage. Apparently, the lack of appropriate lectins specific for sulfated glycans is disadvantage of the current lectin microarray system, whereas several animal lectins [57,75] are known to show affinity to sulfated glycans. Inclusion of anti-carbohydrate antibodies is an alternative approach.…”

Section: Perspective: ''Recombinant Shift''mentioning

confidence: 99%

Lectin‐based structural glycomics: A practical approach to complex glycans

2011

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Glycans exist in nature in various forms of glycoconjugates, i.e., glycoproteins, glycolipids, and glycosaminoglycans, either in soluble or membrane-bound forms. One of their prominent properties distinguished from nucleic acids and proteins is "heterogeneity" largely attributed to their inherent features of biosynthesis. In general, various methods based on the physicochemical principles have been taken for their separation and structural determination although all of them require prior liberation of glycans and appropriate labeling. On the other hand, a series of carbohydrate-binding proteins, or "lectins," have extensively been used in a more direct manner for cell typing, histochemical staining, and glycoprotein fractionation. Although most procedures conventionally used are useful, unfortunately they lack "throughput" comparable to a performance required for current omics studies. Recently, a novel technique called lectin microarray has attracted increasing attention from not only glycoscientists but also researchers in other fields, because it is straightforward and also informative. The method is innovating in that it enables direct approach to glycoconjugates such as glycoproteins and even cells without liberation of glycans from the core substrate, and therefore can be effectively applied for the sake of differential profiling in various fields. Concept, strategy, and technical advancement of lectin microarray are described. Also, as an introduction to glycomics, the authors explain the motivation to challenge this theme.

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Dual Specificity of Langerin to Sulfated and Mannosylated Glycans via a Single C-type Carbohydrate Recognition Domain

Cited by 76 publications

References 44 publications

Methylated glycans as conserved targets of animal and fungal innate defense

Methylated glycans as conserved targets of animal and fungal innate defense

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

Lectin‐based structural glycomics: A practical approach to complex glycans

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