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Open AccessJournal ArticleDOI

Characterization of Sialyloligosaccharide Binding by Recombinant Soluble and Native Cell-associated CD22 EVIDENCE FOR A MINIMAL STRUCTURAL RECOGNITION MOTIF AND THE POTENTIAL IMPORTANCE OF MULTISITE BINDING

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TLDR
Data are presented indicating that full-length native CD22, expressed on the surface of Chinese hamster ovary cells, is structurally and functionally a multimeric protein, demonstrating a higher apparent affinity for multiply sialylated compounds over monosialylation compounds.
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This article is published in Journal of Biological Chemistry.The article was published on 1995-03-31 and is currently open access. It has received 115 citations till now. The article focuses on the topics: Sialic Acid Binding Immunoglobulin-like Lectins & Immunoglobulin superfamily.

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Citations
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Journal ArticleDOI

Siglecs and their roles in the immune system

TL;DR: The postulated functions of the recently discovered CD33-related Siglecs are discussed and the factors that seem to be driving their rapid evolution are considered.
Journal ArticleDOI

Concepts and Principles of O-Linked Glycosylation

TL;DR: The biosynthesis, structures, and functions of O-glycosylation, as a complex posttranslational event, is reviewed and compared and the recent development of novel technologies for glycan analysis promises to yield new insights in the factors that determine site occupancy, structure-function relationship, and the contribution of O -linked sugars to physiological and pathological processes.
Journal ArticleDOI

Sialic acids as ligands in recognition phenomena.

TL;DR: This work presents a summary of the various proteins that can recognize and bind to this family of monosaccharides, comparing and contrasting the structural requirements and mechanisms involved in binding.
Journal ArticleDOI

Siglecs--the major subfamily of I-type lectins.

TL;DR: Siglecs as mentioned in this paper is a family of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features, which appear to have evolved by convergent evolution.
Book ChapterDOI

Sialic Acids in Molecular and Cellular Interactions

TL;DR: The aim of this chapter is to summarize the knowledge about Sias in masking, for example, galactose residues, and to review the progress made during the past few years with respect to Sias as recognition determinants in the adhesion of pathogenic viruses, bacteria, and protozoa, and particularly as binding sites for endogenous cellular interaction molecules.
References
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Journal ArticleDOI

The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence.

TL;DR: Carbohydrate binding properties of a new plant lectin isolated from elderberry bark were studied using the techniques of quantitative precipitation, hapten inhibition, and equilibrium dialysis, suggesting the presence of a hydrophibic interacting region adjacent to the carbohydrate binding site.
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Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin. Dependence on fine structural features.

TL;DR: It was found that the number of Gal residues/cluster and their branching mode are major determinants of binding affinity of ligands to the hepatic lectin on the surface of hepatocytes.
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Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides.

TL;DR: Structural determinants of oligosaccharides affecting interaction with the saccharide-binding sites of two lectins, the agglutinin of M, 120,000 and toxin of 82, 60,000 (RCA* and RCA~I, respectively), isolated from Ricinus communis beans have been examined by performing binding studies with iodinated glycopeptides and their degradation products.
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The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues.

TL;DR: The authors' analyses indicate that the interactions of complex-type Asn-linked chains with the lectin are dependent on sialic acid linkages and are not dependent on either the branching pattern of the mannose residues or the presence of poly-N-acetyllactosamine sequences.
Journal ArticleDOI

The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2–6 sialyltransferase, CD75, on B cells

TL;DR: Evidence is provided that CD22 is directly involved in the cognate interaction between B and T cells, and one of the two CD22 polypeptides, CD22 beta, interacts with a specific ligand on a subpopulation of CD4+ T cells.
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