Ganglioside binding pattern of CD33-related siglecs

Rapoport, E. M.; Mikhalyov, Ilya; Zhang, Jiquan; Crocker, Paul R.; Bovin, Nicolai V.

doi:10.1016/s0960-894x(02)00998-8

Cited by 50 publications

(30 citation statements)

References 23 publications

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“…The adsorption of gangliosides to a 96 well flat bottom plate was performed as described [84]. Briefly, gangliosides were mixed with cholesterol, dissolved in ethanol, added 150 µl/well to the plate and allowed to dry overnight at 20°C.…”

Section: Methodsmentioning

confidence: 99%

Platelets Recognize Brain-Specific Glycolipid Structures, Respond to Neurovascular Damage and Promote Neuroinflammation

et al. 2013

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Platelets respond to vascular damage and contribute to inflammation, but their role in the neurodegenerative diseases is unknown. We found that the systemic administration of brain lipid rafts induced a massive platelet activation and degranulation resulting in a life-threatening anaphylactic-like response in mice. Platelets were engaged by the sialated glycosphingolipids (gangliosides) integrated in the rigid structures of astroglial and neuronal lipid rafts. The brain-abundant gangliosides GT1b and GQ1b were specifically recognized by the platelets and this recognition involved multiple receptors with P-selectin (CD62P) playing the central role. During the neuroinflammation, platelets accumulated in the central nervous system parenchyma, acquired an activated phenotype and secreted proinflammatory factors, thereby triggering immune response cascades. This study determines a new role of platelets which directly recognize a neuronal damage and communicate with the cells of the immune system in the pathogenesis of neurodegenerative diseases.

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Section: Methodsmentioning

confidence: 99%

Platelets Recognize Brain-Specific Glycolipid Structures, Respond to Neurovascular Damage and Promote Neuroinflammation

et al. 2013

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“…From a simple model of the presence or absence of interacting sugars, we would expect Siglec-7 to have similar binding affinities for the b series gangliosides. This has been seen in some studies (22,56); in others there is a clear rank order in binding affinity (22,57). This variation may reflect differences in experimental conditions (in the way the gangliosides are presented, e.g.…”

Section: Discussionmentioning

confidence: 88%

Siglec-7 Undergoes a Major Conformational Change When Complexed with the α(2,8)-Disialylganglioside GT1b

Attrill

Imamura

Sharma

et al. 2006

Journal of Biological Chemistry

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The siglecs are a group of mammalian sialic acid binding receptors expressed predominantly in the immune system. The CD33-related siglecs show complex recognition patterns for sialylated glycans. Siglec-7 shows a preference for ␣(2,8)-disialylated ligands and provides a structural template for studying the key interactions that drive this selectivity. We have co-crystallized Siglec-7 with a synthetic oligosaccharide corresponding to the ␣(2,8)-disialylated ganglioside GT1b. The crystal structure of the complex offers a first glimpse into how this important family of lectins binds the structurally diverse gangliosides. The structure reveals that the C-C loop, a region implicated in previous studies as driving siglec specificity, undergoes a dramatic conformational shift, allowing it to interact with the underlying neutral glycan core of the ganglioside. The structural data in combination with mutagenesis studies show that binding of the ganglioside is driven by extensive hydrophobic contacts together with key polar interactions and that the binding site structure is complementary to preferred solution conformations of GT1b.

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“…1A), the ganglioside GD3 [11], and other disialylated gangliosides [19,21] or the lipooligosaccharide of the HS:19 (GM1 ϩ GT1a ϩ ) Campylobacter jejuni strain [32]. In contrast, the highly related Siglec-9 bound ␣2,3-sialyllactose-PAA but not the ␣2,8-linked disialic acid structure (Fig.…”

Section: Resultsmentioning

confidence: 99%

Probing the cis interactions of the inhibitory receptor Siglec-7 with α2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of α2,8-sialyltransferase gene expression

Avril

North

Haslam

et al. 2006

Journal of Leukocyte Biology

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Ganglioside binding pattern of CD33-related siglecs

Cited by 50 publications

References 23 publications

Platelets Recognize Brain-Specific Glycolipid Structures, Respond to Neurovascular Damage and Promote Neuroinflammation

Platelets Recognize Brain-Specific Glycolipid Structures, Respond to Neurovascular Damage and Promote Neuroinflammation

Siglec-7 Undergoes a Major Conformational Change When Complexed with the α(2,8)-Disialylganglioside GT1b

Probing the cis interactions of the inhibitory receptor Siglec-7 with α2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of α2,8-sialyltransferase gene expression

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