Specificity of DC‐SIGN for mannose‐ and fucose‐containing glycans

Liempt, Ellis van; Bank, Christine M C; Mehta, Padmaja; ́a-Vallejo, Juan Jesús Garcı; Kawar, Ziad; Geyer, Rudolf; Alvarez, Richard A.; Cummings, Richard D.; Kooyk, Yvette van; Die, Irma van

doi:10.1016/j.febslet.2006.10.009

Cited by 251 publications

(226 citation statements)

References 37 publications

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“…From a biological point of view, the most important characteristics of the FVIII/VWF complex is to show specificity for different carbohydrates and to show certain flexibility of the binding sites that would allow for the recognition of a range of structurally related carbohydrates as a regulation mechanism similar to that of other reported lectins (Vasta et al 1994;Hernández et al 2004). Vertebrate lectins fall into a number of structurally distinct families and participate in different intracellular functions, such as trafficking, sorting, and targeting of maturing glycoproteins, (Dodd and Drickamer 2001) as well as in extracellular functions, such as adhesive interactions (Zelensky and Gready 2005), by mediating interaction with the extracellular matrix or body fluids, or by mediating cell adhesion, cell signaling, inducing gene transcription, post-translational modifications, glycoprotein clearance, and pathogen recognition (Britten et al 1998;van Liempt et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Santizo

Zenteno

Pina-Canseco

et al. 2009

Tohoku J. Exp. Med.

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The human coagulation factor VIII (FVIII) is an essential cofactor for the proteolytic activation of factor X. FVIII is activated by thrombin and blood coagulation factor Xa; factor IXa (FIXa) activates factor X (FXa), requiring Ca 2+ , phospholipids, and activated Factor VIII (FVIIIa) (Schmidt et al. 2005). FVIII and von Willebrand factor (VWF) form a non-covalently bound complex. This complex (FVIII/ VWF) circulates in the human plasma, is critical to homeostasis, and normally exists in inactive form. The binding of FVIII to VWF is essential for the survival of FVIII in vivo (Kaufman and Pipe 1999). Deficiencies or structural defects in FVIII are responsible for the most common inherited bleeding disorders, such as hemophilia and von Willebrand disease (Lillicrap 2008).FVIII is a polypeptide of 2332 amino acids, synthesized in the liver by parenchyma cells and hepatic sinusoidal endothelium cells, as well as by the pulmonary endothelium. FVIII has several glycosylation sites that appear to be important in its circulation kinetics. This factor possesses N-glycosydically linked glycans, which are characterized by a N-acetyl-glucosamine (GlcNAc)-asparagine inner core and are relevant for the folding and productive secretion of FVIII, and O-glycosydically glycans, which are characterized by N-acetyl-galactosamine (GalNAc)-serine/threonine and are involved in determining protein conformation and interact with other glycoproteins. FVIII possesses two unusual mannosylated sites that can be recognized by mannose receptors on Kupffer cells (Dasgupta et al. 2007).

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Section: Discussionmentioning

confidence: 99%

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Santizo

Zenteno

Pina-Canseco

et al. 2009

Tohoku J. Exp. Med.

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“…DC-SIGN is also able to recognize branched fucosylated structures with terminal galactose residues, such as the Lewis antigens. This binding interaction on macrophages activates phagocytosis [48]. …”

Section: Dc-sign Inhibitors As Viral Anti-adhesivesmentioning

confidence: 99%

Exploitation of Glycobiology in Anti-Adhesion Approaches against Biothreat Agents

Utratna¹,

Deegan²,

Joshi³

2016

J Bioterror Biodef

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Pathogen adherence to a host cell is one of the first essential steps for establishing invasion, colonization and release of virulence factors such as toxins. Understanding the mechanisms used by pathogens and toxins to adhere and invade human cells could lead to the development of new strategies for preventing and controlling the spread of infectious diseases. This review focuses on carbohydrate-lectin interactions utilized by selected biothreat agents to bind and invade host cells. The principle of using anti-adhesion molecules, based on glycobiology research, has already been shown to be effective in the treatment of influenza. Therefore, translating the same principle to other biothreat agents that mediate invasion of a host cell through carbohydrate-lectin mechanisms is a very promising strategy. We investigate recent literature to highlight the latest developments in the field of glycobiology focused on inhibiting the initial steps of pathogen invasion, with examples for bacteria, toxin and virus interactions. The successful glycomimetics and glycoconjugates represent strategies for interruption of adhesion by single molecules and in multivalent systems against uropathogenic E. coli, several toxins (Shiga-like, cholera, botulinum) and wellknown or emerging viruses (influenza, HIV, Ebola, and Zika). This review provides promising directions and prophylactic as well as therapeutic potential of anti-adhesive strategies against selected biothreat targets.

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“…It should be noted that the mere presence of a potential CLR-binding ligand does not necessarily indicate binding-or functional activity, which should be experimentally established. For example, whereas high-mannose glycans are DC-SIGN ligands (77) and S. mansoni SEA contain high-mannose glycans, the major ligands for DC-SIGN on SEA are Le X and LDNF (71). For DC-SIGN elucidation of the crystal structure, in combination with studies on the interaction of the carbohydrate-recognition domain (CRD) with different glycan ligands, demonstrated that the structure of the glycan and its multivalency of presentation, as well as the docking of the glycan in the CRD(s) of the lectin, determine whether a high-affinity or high-avidity binding is established with a particular lectin (Fig.…”

Section: Can Helminth Compounds Suppress Inflammatory Responses Of DCmentioning

confidence: 99%

Worms to the rescue: Can worm glycans protect from autoimmune diseases?

Kuijk

Die

2010

IUBMB Life

Self Cite

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Autoimmune and autoinflammatory diseases represent a significant health burden, especially in Western societies. For the majority of these diseases, no cure exists. Recently, research on parasitic worms (helminths) has demonstrated great potential for whole worms, their eggs or their excretory/secretory proteins in down‐regulating inflammatory responses both in vitro and in vivo, in various disease models and, in some cases, even in clinical trials. The worms are thought to induce Th2 and regulatory T cells, interfere with Toll‐like receptor (TLR) signaling and to down‐regulate Th17 and Th1 responses. The molecular mechanisms underlying the worms' ability to modulate the host immune response are not well understood, and many hypotheses have been proposed to explain the observed immune modulation. Increasing evidence suggests that carbohydrate structures (glycans), for example, phosphorylcholine‐modified glycans or Galβ1‐4(Fucα1‐3)GlcNAc‐ (Lewis X, LeX) containing glycans, expressed by the worms contribute to these modulating properties by their interaction with antigen presenting cells. Helminths express a broad variety of protein‐ and lipid‐linked glycans on their surface and on secretory products. These glycans differ in amount and composition and several of these structures are species specific. However, worms also express glycan antigens that are found in a wide variety of different species. Some of these “common” worm glycans are particularly interesting with regard to regulating host responses, because they have the potential to interact with C‐type lectins on dendritic cells and thereby may interfere with T‐cell polarization. Helminths and helminth‐derived molecules form a novel and promising group of therapeutics for autoinflammatory diseases. However, much has to be learned about the molecular mechanisms behind the helminth‐mediated antiinflammatory properties. This review will describe some of the emerging evidence in selected disease areas as well as discuss the putative role of glycans in helminth‐mediated immunosuppression. © 2010 IUBMB IUBMB Life, 62(4): 303–312, 2010

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Specificity of DC‐SIGN for mannose‐ and fucose‐containing glycans

Cited by 251 publications

References 37 publications

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Exploitation of Glycobiology in Anti-Adhesion Approaches against Biothreat Agents

Worms to the rescue: Can worm glycans protect from autoimmune diseases?

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