Carbohydrate microarrays reveal sulphation as a modulator of siglec binding

Campanero-Rhodes, María Asunción; Childs, Robert A.; Kiso, M.; Komba, Shiro; Narvor, Christine Le; Warren, Joanna; Otto, Diana M. E.; Crocker, Paul R.; Feizi, Ten

doi:10.1016/j.bbrc.2006.03.223

Cited by 89 publications

(89 citation statements)

References 20 publications

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“…GlcNAc 6-sulfate even serves as a ligand for siglecs, such as CD22 (Siglec-2) (27,28) and Siglec-9 (29). In contrast, the functional importance of Gal 6-sulfate is much less understood, although Gal-6-sulfated sialyl Lewis X was shown to be a candidate ligand for Siglec-8 (30) and its mouse paralog, Siglec-F (29,31). In 2004, Galustian et al (11) reported binding activity of Langerin to sulfated Lewis X glycans, although the importance of sulfation on Langerin recognition has not been fully elucidated.…”

Section: Discussionmentioning

confidence: 99%

“…GlcNAc 6-sulfate is involved in several recognition phenomena, including selectin-mediated lymphocyte homing (24), activation of CD44-mediated cellular interaction (25), and dendritic cell function (26). GlcNAc 6-sulfate even serves as a ligand for siglecs, such as CD22 (Siglec-2) (27,28) and Siglec-9 (29). In contrast, the functional importance of Gal 6-sulfate is much less understood, although Gal-6-sulfated sialyl Lewis X was shown to be a candidate ligand for Siglec-8 (30) and its mouse paralog, Siglec-F (29,31).…”

Section: Discussionmentioning

confidence: 99%

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

Tateno

Ohnishi

Yabe

et al. 2010

Journal of Biological Chemistry

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Langerin is categorized as a C-type lectin selectively expressed in Langerhans cells, playing roles in the first line of defense against pathogens and in Birbeck granule formation. Although these functions are thought to be exerted through glycan-binding activity of the C-type carbohydrate recognition domain, sugar-binding properties of Langerin have not been fully elucidated in relation to its biological functions. Here, we investigated the glycan-binding specificity of Langerin using comprehensive glycoconjugate microarray, quantitative frontal affinity chromatography, and conventional cell biological analyses. Langerin showed outstanding affinity to galactose-6-sulfated oligosaccharides, including keratan sulfate, while it preserved binding activity to mannose, as a common feature of the C-type lectins with an EPN motif. By a mutagenesis study, Lys-299 and Lys-313 were found to form extended binding sites for sulfated glycans. Consistent with the former observation, the sulfated Langerin ligands were found to be expressed in brain and spleen, where the transcript of keratan sulfate 6-O-sulfotransferase is expressed. Moreover, such sulfated ligands were up-regulated in glioblastoma relative to normal brain tissues, and Langerin-expressing cells were localized in malignant brain tissues. Langerin also recognized pathogenic fungi, such as Candida and Malassezia, expressing heavily mannosylated glycans. These observations provide strong evidence that Langerin mediates diverse functions on Langerhans cells through dual recognition of sulfated as well as mannosylated glycans by its uniquely evolved C-type carbohydrate-recognition domain.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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

Tateno

Ohnishi

Yabe

et al. 2010

Journal of Biological Chemistry

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“…Thus, carbohydrate microarrays have been successfully used for detection and quantitation of disease-associated anticarbohydrate antibodies and analysis of their binding specicity, [20][21][22] and for identication of oligosaccharide signals recognized by endogenous lectins, as C-type lectins, [23][24][25] siglecs [26][27][28] and galectins, or by pathogens' glycan-binding proteins that mediate docking into host cells.…”

Section: -19mentioning

confidence: 99%

“…1 ml ml À1 of Cy3 uorophore (GE Healthcare) was added to the protein solutions to enable post-array monitoring of the spots, 27 by scanning uorescence signals upon excitation at 532 nm (green laser). Following the binding assay, arrays were scanned for both AF647 (excitation at 635 nm, red laser) and SYTO-13 uores-cence signals.…”

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confidence: 99%

Bacteria microarrays as sensitive tools for exploring pathogen surface epitopes and recognition by host receptors

et al. 2015

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We describe a protocol for the generation and validation of bacteria microarrays and their application to the study of specific features of the pathogen's surface and interactions with host receptors. Bacteria were directly printed on nitrocellulose-coated glass slides, using either manual or robotic arrayers, and printing quality, immobilization efficiency and stability of the arrays were rigorously controlled by screening/evaluation of compounds to identify inhibitors of host-pathogen interactions, make bacteria microarrays a useful and sensitive tool for both basic and applied research in microbiology, biomedicine and biotechnology.

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“…41 Multivalent formats for the study of selective recognition by Siglecs have been also achieved following pre-complexation of mSiglecs-Fc and hSiglecs-Fc with the corresponding antibodies. [45][46][47] The need of the formation of a precomplex Siglec-Fc-antibody to observe binding between Siglecs and recognition ligands was also reported, despite the bivalency of the tested Siglec-Fc, when polyacrylamide probe beads with pendant carbohydrate ligands were used for the recognition of Siglecs. 36 In the research presented here, the multivalent presentation of the Siglecs was achieved by crosslinking the different dimeric Siglec-Fc chimaeric proteins with an anti-Fc-IgG antibody.…”

Section: Plasmonic Detection Of Siglecs In Solution Using the Glyconamentioning

confidence: 99%

Detection of mSiglec-E, in solution and expressed on the surface of Chinese hamster ovary cells, using sialic acid functionalised gold nanoparticles

Schofield

Marín

Rejzek

et al. 2016

Analyst

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Sialic acids are widespread in biology, fulfilling a wide range of functions. Their cognate lectin receptors -Siglecs -are equally diverse and widely distributed, with different Siglecs found within distinct populations of cells in the haemopoietic, immune and nervous systems. A convenient way to assay ligand recognition of soluble Siglecs would be useful, as would methods for the concomitant assessment of Siglec distribution on cell surfaces. Here we report the use of gold nanoparticles functionalised with a sialic acid ligand diluted with a polyethylene glycol (PEG) ligand for the plasmonic detection of a soluble form of murine Siglec-E (mSiglec-E-Fc fusion protein) and, importantly, for the specific detection of the same siglec expressed on the surface of mammalian cells. These sialic acid functionalised nanoparticles are shown to overcome problems such as cellular cis interactions and low Siglec-ligand affinity. The gold nanoparticles were functionalised with various ratios of sialic acid:PEG ligands and the optimum ratio for the detection of murine Siglec-E was established based on the plasmonic detection of the soluble pre-complexed recombinant form of murine Siglec-E (mSiglec-E-Fc fusion protein). The optimum ratio for the detection of the fusion protein was found to be sialic acid:PEG ligands in a 50:50 ratio (glyconanoparticles 1).The optimised glyconanoparticles 1 were used to recognise and bind to the murine Siglec-E expressed on the surface of transfected Chinese hamster ovary cells as determined by transmission electron microscopy.3

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Carbohydrate microarrays reveal sulphation as a modulator of siglec binding

Cited by 89 publications

References 20 publications

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

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

Bacteria microarrays as sensitive tools for exploring pathogen surface epitopes and recognition by host receptors

Detection of mSiglec-E, in solution and expressed on the surface of Chinese hamster ovary cells, using sialic acid functionalised gold nanoparticles

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