Neoglycolipid Probes Prepared via Oxime Ligation for Microarray Analysis of Oligosaccharide-Protein Interactions

Liu, Yan; Feizi, Ten; Campanero-Rhodes, María Asunción; Childs, Robert A.; Zhang, Yibing; Mulloy, Barbara; Evans, Philip G.; Osborn, Helen M. I.; Otto, Diana M. E.; Crocker, Paul R.; Chai, Wengang

doi:10.1016/j.chembiol.2007.06.009

Cited by 127 publications

(125 citation statements)

References 61 publications

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“…This is in overall agreement with previous findings (1). Although the oligosaccharide sequences of probes 18, 20, 21, and 22 are short tri-or tetrasaccharides, their recognition demonstrates the effective presentation of these as oxime-linked neoglycolipids on the array surface (30).…”

Section: Binding Properties Of Other T Gondii Proteins Of the Mar Dosupporting

confidence: 92%

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Friedrich

Santos

Liu

et al. 2010

Journal of Biological Chemistry

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Numerous intracellular pathogens exploit cell surface glycoconjugates for host cell recognition and entry. Unlike bacteria and viruses, Toxoplasma gondii and other parasites of the phylum Apicomplexa actively invade host cells, and this process critically depends on adhesins (microneme proteins) released onto the parasite surface from intracellular organelles called micronemes (MIC). The microneme adhesive repeat (MAR) domain of T. gondii MIC1 (TgMIC1) recognizes sialic acid (Sia), a key determinant on the host cell surface for invasion by this pathogen. By complementation and invasion assays, we demonstrate that TgMIC1 is one important player in Sia-dependent invasion and that another novel Sia-binding lectin, designated TgMIC13, is also involved. Using BLAST searches, we identify a family of MAR-containing proteins in enteroparasitic coccidians, a subclass of apicomplexans, including T. gondii, suggesting that all these parasites exploit sialylated glycoconjugates on host cells as determinants for enteric invasion. Furthermore, this protein family might provide a basis for the broad host cell range observed for coccidians that form tissue cysts during chronic infection. Carbohydrate microarray analyses, corroborated by structural considerations, show that TgMIC13, TgMIC1, and its homologue Neospora caninum MIC1 (NcMIC1) share a preference for ␣2-3-over ␣2-6-linked sialyl-N-acetyllactosamine sequences. However, the three lectins also display differences in binding preferences. Intense binding of TgMIC13 to ␣2-9-linked disialyl sequence reported on embryonal cells and relatively strong binding to 4-O-acetylated-Sia found on gut epithelium and binding of NcMIC1 to 6sulfo-sialyl Lewis x might have implications for tissue tropism. Sialic acids (Sias)6 occur abundantly in glycoproteins and glycolipids on the cell surface and are exploited by many viruses and bacteria for attachment and host cell entry. Recognition of carbohydrates and in particular sialylated glycoconjugates is important also for host cell invasion by the Apicomplexa (1-4), a phylum that includes several thousand species of obligate intracellular parasites, among them the Plasmodium spp. causing malaria. Enteroparasitic coccidians are a subclass of Apicomplexa comprising Eimeria spp. responsible for coccidiosis in poultry, Neospora spp. causing neosporosis in cattle, and Toxoplasma, the causative agent of toxoplasmosis in warmblooded animals and humans.The host range and cell type targeted by these parasites vary widely across the phylum. Whereas Plasmodium falciparum merozoites exclusively invade erythrocytes of humans and great apes (5), Toxoplasma gondii tachyzoites (the form of the parasite associated with acute infection) invade an extremely broad range of cell types in humans and virtually all warmblooded animals, enabling rapid establishment of infection in the host and dissemination into deep tissues (6). Information is emerging on the involvement of carbohydrate-protein interactions in this broad host cell recognition (1).Many intracellular...

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Section: Binding Properties Of Other T Gondii Proteins Of the Mar Dosupporting

confidence: 92%

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Friedrich

Santos

Liu

et al. 2010

Journal of Biological Chemistry

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“…However, Siglec-E bound to α2,8-disialic acid more strongly than to α2,3-sialyllactose and bound weakly to α2,6-sialyllactose on polyacrylamide [55]. This binding pattern of Siglec-E to glycolipids and gangliosides differs from that of Siglec-9 [69].…”

Section: Natural Ligands For Siglec-9 and Siglec-ementioning

confidence: 78%

Targeting Neutrophils in Severe Asthma via Siglec-9

Chen

Bai

Han

et al. 2018

Int Arch Allergy Immunol

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Severe asthma comprises only 5% of patients with asthma, but the burden it brings to the social health system accounts for more than half of all asthmatics. Clinical evidence shows that severe asthma is often linked to the recruitment and activation of neutrophils in the airways. However, the underlying molecular and immunological mechanisms of neutrophilia in severe asthma are not clear and currently available drugs exert only limited effects on neutrophilic inflammation. Great efforts are underway to address the mystery of neutrophilic inflammation in chronic respiratory disorders. Sialic acid-binding immunoglobulin-like lectins (Siglecs) are members of the immunoglobulin gene family. Of note, Siglec-9 is uniquely expressed by human neutrophils and monocytes, as well as a minor population of natural killer cells. Engaging this structure with antibodies or glycan ligands results in programmed cell death in human neutrophils. Intriguingly, the administration of Siglec-E antibody abolished the recruitment of neutrophils in mouse models of neutrophilic pulmonary inflammation in vivo. Given that neutrophils are probably a major culprit in the generation and perpetuation of inflammation, targeting Siglec-9 could be beneficial for the treatment of severe asthma, chronic obstructive pulmonary disease, and related pulmonary disorders characteristic of neutrophilia.

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“…[1][2][3] Solid-phase chemical methods are gaining importance as a tool enabling the study of these processes. [4] Chemoselective coupling of unprotected carbohydrates to, for example, polymeric supports, [5][6][7] microarrays, [8][9][10] peptides and proteins, [11] and to other surfaces [12] through oxime formation has been widely exploited in recent years as a means to capture glycans from natural sources and to obviate laborious glycosylation and protecting-group chemistry. The reaction exploits the unique availability of an aldehyde moiety in the reducing-end of glycans, which also allows, for example, reductive amination, hydrazone and acyl hydrazone formation, and thiazolidine formation.…”

Section: Introductionmentioning

confidence: 99%

Chemoselective Capture of Glycans for Analysis on Gold Nanoparticles: Carbohydrate Oxime Tautomers Provide Functional Recognition by Proteins

Thygesen¹,

Sauer²,

Jensen³

2009

Chemistry A European J

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Nanoparticles functionalized with glycans are emerging as powerful solid-phase chemical tools for the study of protein-carbohydrate interactions using nanoscale properties for detection of binding events. Methods or reagents that enable the assembly of glyconanoparticles from unprotected glycans in two consecutive chemoselective steps with meaningful display of the glycan are highly desirable. Here, we describe a novel bifunctional reagent that 1) couples to glycans by oxime formation in solution, 2) aids in purification through a lipophilic trityl tag, and 3) after deprotection then couples to gold nanoparticles through a thiol. NMR studies revealed that these oximes exist as both the open-chain and N-glycosyl oxy-amine tautomers. Glycan-linker conjugates were coupled through displacement of ligands from preformed, citrate-stabilized gold nanoparticles. Recognition of these glycans by proteins was studied with a lectin, concanavalin A (ConA), in an aggregation assay and with a processing enzyme and glucoamylase (GA). We demonstrate that the presence of the N-glycosyl oxy-amines clearly enables functional recognition in sharp contrast to the corresponding reduced oxy-amines. This concept is then realized in a novel reagent, which should facilitate nanoglycobiology by enabling the operationally simple capture of glycans and their biologically meaningful display.

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Neoglycolipid Probes Prepared via Oxime Ligation for Microarray Analysis of Oligosaccharide-Protein Interactions

Cited by 127 publications

References 61 publications

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Targeting Neutrophils in Severe Asthma via Siglec-9

Chemoselective Capture of Glycans for Analysis on Gold Nanoparticles: Carbohydrate Oxime Tautomers Provide Functional Recognition by Proteins

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