title: Role of siglecs and related glycan-binding proteins in immune responses and immunoregulation.
abstract: Virtually all cells and extracellular material are heavily decorated by various glycans, yet our understanding of the structure and function of these moieties lags behind the understanding of nucleic acids, lipids, and proteins. Recent years have seen a tremendous acceleration of knowledge in the field of glycobiology, revealing many intricacies and functional contributions that were previously poorly appreciated or even unrecognized. This review highlights several topics relevant to glycoimmunology in which mammalian and pathogen-derived glycans displayed on glycoproteins and other scaffolds are recognized by specific glycan-binding proteins (GBPs), leading to a variety of proinflammatory and anti-inflammatory cellular responses. The focus for this review is mainly on 2 families of GBPs, sialic acid-binding immunoglobulin-like lectins (siglecs) and selectins, that are involved in multiple steps of the immune response, including distinguishing pathogens from self, cell trafficking to sites of inflammation, fine-tuning of immune responses leading to activation or tolerance, and regulation of cell survival. Importantly for the clinician, accelerated rates of discovery in the field of glycoimmunology are being translated into innovative medical approaches that harness the interaction of glycans and GBPs to the benefit of the host and might soon lead to novel diagnostics and therapeutics.
authors.affiliation: Department of Medicine, Division of Allergy-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Ill. Electronic address: bruce.bochner@northwestern.edu.
authors.forename: Bruce S
authors.initials: BS
authors.lastname: Bochner
authors.affiliation: Department of Pediatrics, Division of Allergy and Immunology, Children's Hospital Medical Center, and Department of Pathology, University of Cincinnati College of Medicine, Cincinnati, Ohio.
authors.forename: Nives
authors.initials: N
authors.lastname: Zimmermann
mesh_terms: D000818:Animals; D005786:Gene Expression Regulation / Q000276:immunology*; D015658:HIV Infections / Q000235:genetics / Q000276:immunology / Q000473:pathology; D006801:Humans; D006967:Hypersensitivity / Q000235:genetics / Q000276:immunology / Q000473:pathology; D007113:Immunity, Innate; D007249:Inflammation / Q000235:genetics / Q000276:immunology / Q000473:pathology; D009369:Neoplasms / Q000235:genetics / Q000276:immunology / Q000473:pathology; D011008:Pneumococcal Infections / Q000235:genetics / Q000276:immunology / Q000473:pathology; D011134:Polysaccharides / Q000737:chemistry / Q000276:immunology*; D011485:Protein Binding; D017382:Reactive Oxygen Species / Q000276:immunology; D012552:Schistosomiasis / Q000235:genetics / Q000276:immunology / Q000473:pathology; D019087:Selectins / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D063265:Sialic Acid Binding Immunoglobulin-like Lectins / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D015398:Signal Transduction
chemical_list: D011134:Polysaccharides; D017382:Reactive Oxygen Species; D019087:Selectins; D063265:Sialic Acid Binding Immunoglobulin-like Lectins
keywords: Siglec; dectin; glycan; glycan-binding proteins; glycobiology; selectin; sialic acid; treatment