Multiple Modes of Binding Enhance the Affinity of DC-SIGN for High Mannose N-Linked Glycans Found on Viral Glycoproteins

Feinberg, H.; Castelli, Riccardo; Drickamer, Kurt; Seeberger, Peter H.; Weis, William I.

doi:10.1074/jbc.m609689200

Cited by 159 publications

(221 citation statements)

References 29 publications

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“…S6), suggesting that the complex CA-mannan moiety might not bind to DC-SIGN as conventional high mannose oligosaccharides. The binding of DC-SIGN to synthetic fragments of high mannose oligosaccharides has been shown to occur via multiple modes that may involve different amino acids and further enhance the receptor avidity (56,57). Moreover, the intrinsic oligomerization of DC-SIGN (58) and its tendency to form nanoclusters (59) are likely to provide additional regulation levels for the interaction of DC-SIGN with this type of fungal mannan arrays.…”

Section: Discussionmentioning

confidence: 99%

Dendritic Cell Interaction with Candida albicans Critically Depends on N-Linked Mannan

Cambi

Netea

Mora-Montes

et al. 2008

Journal of Biological Chemistry

215

208

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The fungus Candida albicans is the most common cause of mycotic infections in immunocompromised hosts. Little is known about the initial interactions between Candida and immune cell receptors, because a detailed characterization at the structural level is lacking. Antigen-presenting dendritic cells (DCs), strategically located at mucosal surfaces and in the skin, may play an important role in anti-Candida protective immunity. However, the contribution of the various Candida-associated molecular patterns and their counter-receptors to DC function remains unknown. Here, we demonstrate that two C-type lectins, DC-SIGN and the macrophage mannose receptor, specifically mediate C. albicans binding and internalization by human DCs. Moreover, by combining a range of C. albicans glycosylation mutants with receptor-specific blocking and cytokine production assays, we determined that N-linked mannan but not O-linked or phosphomannan is the fungal carbohydrate structure specifically recognized by both C-type lectins on human DCs and directly influences the production of the proinflammatory cytokine IL-6. Better insight in the carbohydrate recognition profile of C-type lectins will ultimately provide relevant information for the development of new drugs targeting specific fungal cell wall antigens.

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Section: Discussionmentioning

confidence: 99%

Dendritic Cell Interaction with Candida albicans Critically Depends on N-Linked Mannan

Cambi

Netea

Mora-Montes

et al. 2008

Journal of Biological Chemistry

215

208

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“…The glycans interact primarily with a Ca 2+ ion exposed at the surface of DC-SIGN carbohydrate recognition domain (CRD). X-ray data are available for complexes of DC-SIGN CRD with mannose oligosaccharides, and with the fucosylated oligosaccharide Lewis X [40][41][42][43]. blocking viral adhesion and entry in sexually transmitted HIV infection.…”

Section: Prophylactic Antiviral Agents Targeting Dc-signmentioning

confidence: 99%

Glycoconjugates and Glycomimetics as Microbial Anti-Adhesives

Sattin

Bernardi

2016

Trends in Biotechnology

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Microbial adhesion is an essential step of infections and is mediated primarily by proteincarbohydrate interactions. Antagonists of such interactions have become a promising target for antiadhesive therapy in a number of infective diseases. Monovalent protein-sugar interactions are often weak, and most successful antiadhesive materials consist of multivalent glycoconjugates.Although often very effective in hampering microbial adhesion, natural epitopes often show limited resistance to enzymatic degradation. The use of carbohydrate mimics (glycomimetics) as a replacement for natural sugars potentially allows to achieve higher metabolic stability and also higher selectivity towards the desired protein target. In this review we will describe the state of the art on the design and synthesis of glycoconjugates and glycomimetics employed for the construction of antiadhesive biomaterials.

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“…The primary interaction of oligosaccharides and DC-SIGN occurs by coordination of a residue of the oligosaccharide (often the non-reducing end) to a Ca 2+ binding site exposed to the surface of the protein (Feinberg et al, 2001;Guo et al, 2004;Feinberg et al, 2007). X-ray data are available for complexes of the DC-SIGN carbohydrate recognition domain (CRD) with both mannose oligosaccharides and Lewis-X (Feinberg et al, 2001;Guo et al, 2004;Feinberg et al, 2007).…”

Section: Dc-signmentioning

confidence: 99%

“…X-ray data are available for complexes of the DC-SIGN carbohydrate recognition domain (CRD) with both mannose oligosaccharides and Lewis-X (Feinberg et al, 2001;Guo et al, 2004;Feinberg et al, 2007). Besides the role that DC-SIGN plays in infection processes, the recent discovery of DC-SIGN as a lectin involved in immunoregulation processes attracted the interest of many scientists due to the possibility to exploit this lectin as a new potential target in immunotherapy.…”

Section: Dc-signmentioning

confidence: 99%

Glycodendritic structures: tools to interact with DC-SIGN

Reina

Rojo

2013

Braz. J. Pharm. Sci.

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The key role of carbohydrates in many biological events has attracted the interest of the scientific community. This fact has demanded the access to new tools necessary to understand this role and the interaction of carbohydrates with their corresponding receptors, lectins. Glycodendrimers and glycodendritic structures in general, have demonstrated to be very efficient and interesting tools to intervene in those processes where carbohydrates participate. In this review, we discuss the different glycodendritic structures that have been used to interfere with DC-SIGN, a very attractive lectin involved in infection processes and in the regulation of the immune response.

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Multiple Modes of Binding Enhance the Affinity of DC-SIGN for High Mannose N-Linked Glycans Found on Viral Glycoproteins

Cited by 159 publications

References 29 publications

Dendritic Cell Interaction with Candida albicans Critically Depends on N-Linked Mannan

Dendritic Cell Interaction with Candida albicans Critically Depends on N-Linked Mannan

Glycoconjugates and Glycomimetics as Microbial Anti-Adhesives

Glycodendritic structures: tools to interact with DC-SIGN

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