Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms

Davicino, Roberto; Eliçabe, Ricardo Javier; Genaro, María Silvia Di; Rabinovich, Gabriel A.

doi:10.1016/j.intimp.2011.05.002

Cited by 64 publications

(48 citation statements)

References 77 publications

(130 reference statements)

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“…Furthermore, as galectin-ligand interactions are relatively weak compared with other immune recognition molecules, high avidity for the target is achieved by the multiple CRDs simultaneously interacting with ligand. Therefore, the 4-CRD galectins (and to a lesser extent the 2-CRD galectins) from aquatic mollusk species may have the potential for cooperative, high avidity binding as well as cross-linking of the recognized microbial glycans with the hemocyte surface, leading to their opsonization and phagocytosis [57, 88, 89]. Further, the binding of the multiple CRD galectins to glycans on the hemocyte surface would facilitate glycan crosslinking and lattice formation, which trigger signaling pathways leading to cell activation [15, 90].…”

Section: Galectins In Aquatic Mollusksmentioning

confidence: 99%

Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse

Vasta

Feng

Bianchet

et al. 2015

Fish & Shellfish Immunology

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Galectins constitute a conserved and widely distributed lectin family characterized by their binding affinity for β-galactosides and a unique binding site sequence motif in the carbohydrate recognition domain (CRD). In spite of their structural conservation, galectins display a remarkable functional diversity, by participating in developmental processes, cell adhesion and motility, regulation of immune homeostasis, and recognition of glycans on the surface of viruses, bacteria and protozoan parasites. In contrast with mammals, and other vertebrate and invertebrate taxa, the identification and characterization of bona fide galectins in aquatic mollusks has been relatively recent. Most of the studies have focused on the identification and domain organization of galectin-like transcripts or proteins in diverse tissues and cell types, including hemocytes, and their expression upon environmental or infectious challenge. Lectins from the eastern oyster Crassostrea virginica, however, have been characterized in their molecular, structural and functional aspects and some notable features have become apparent in the galectin repertoire of aquatic mollusks. These including less diversified galectin repertoires and different domain organizations relative to those observed in vertebrates, carbohydrate specificity for blood group oligosaccharides, and up regulation of galectin expression by infectious challenge, a feature that supports their proposed role(s) in innate immune responses. Although galectins from some aquatic mollusks have been shown to recognize microbial pathogens and parasites and promote their phagocytosis, they can also selectively bind to phytoplankton components, suggesting that they also participate in uptake and intracellular digestion of microalgae. In addition, the experimental evidence suggests that the protozoan parasite Perkinsus marinus has co-evolved with the oyster host to be selectively recognized by the oyster hemocyte galectins over algal food or bacterial pathogens, thereby subverting the oyster’s innate immune/feeding recognition mechanisms to gain entry into the host cells.

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Section: Galectins In Aquatic Mollusksmentioning

confidence: 99%

Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse

Vasta

Feng

Bianchet

et al. 2015

Fish & Shellfish Immunology

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“…These lectins are found in almost all organisms and to date 15 galectins have been found in mammals; although only 12 galectin genes are found in humans. On the basis of their molecular structure, galectins are classified into three main types: 'proto-type' galectins, comprising a single polypeptide chain that is able to dimerize (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15); "tandem repeat-type" galectins, composed of a single polypeptide chain presenting two CRDs connected by a linker peptide (galectin-4, -6, -8, -9, and -12); and the "chimera-type" galectin-3, which consists of one C-terminal CRD linked to an N- (Davicino, Elicabe et al 2011). …”

Section: Galectinsmentioning

confidence: 99%

Galectins: new agonists of platelet activation

Schattner

Rabinovich²

2013

Biological Chemistry

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SummaryPlatelet activation at sites of vascular injury leads to the formation of a hemostatic plug and is crucial for hemostasis. However, uncontrolled platelet activation may lead to the formation of occlusive thrombi. Several soluble or matricellular proteins can activate platelets. In this article we review recent advances on the role of galectins in platelet physiology. Either in soluble or immobilized form, these endogenous glycan-binding proteins trigger platelet activation through modulation of discrete signaling pathways. We discuss the role of platelet-galectin interactions not only in hemostasis, but also in chronic inflammation, atherosclerosis and cancer.

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“…Also in mammalian hosts, various types of lectins can recognize glycans that are typically found on pathogens, but not on host cells, such as mannose binding protein and dectin-1 that bind high mannose and β-glucan ligands, respectively, on yeast (5–8). Thus, these types of lectins have been grouped in the category of pattern recognition receptors (PRRs) that bind pathogen-associated molecular patterns (PAMPs) expressed exclusively on microbes (9, 10). …”

Section: Introductionmentioning

confidence: 99%

Microbeâ€“Host Interactions are Positively and Negatively Regulated by Galectinâ€“Glycan Interactions

et al. 2014

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Microbe–host interactions are complex processes that are directly and indirectly regulated by a variety of factors, including microbe presentation of specific molecular signatures on the microbial surface, as well as host cell presentation of receptors that recognize these pathogen signatures. Cell surface glycans are one important class of microbial signatures that are recognized by a variety of host cell lectins. Host cell lectins that recognize microbial glycans include members of the galectin family of lectins that recognize specific glycan ligands on viruses, bacteria, fungi, and parasites. In this review, we will discuss the ways that the interactions of microbial glycans with host cell galectins positively and negatively regulate pathogen attachment, invasion, and survival, as well as regulate host responses that mitigate microbial pathogenesis.

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Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms

Cited by 64 publications

References 77 publications

Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse

Structural, functional, and evolutionary aspects of galectins in aquatic mollusks: From a sweet tooth to the Trojan horse

Galectins: new agonists of platelet activation

Microbeâ€“Host Interactions are Positively and Negatively Regulated by Galectinâ€“Glycan Interactions

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