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Related Concept Videos

Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Glycosaminoglycans01:23

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

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Rapid Glyco-Qualitative Assessment of Recombinant Proteins Using a Fully Automated System
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Human tandem-repeat-type galectins bind bacterial non-βGal polysaccharides.

Yu A Knirel1, H-J Gabius, O Blixt

  • 1N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prosp., 47, Moscow, 119991, Russian Federation.

Glycoconjugate Journal
|September 26, 2013
PubMed
Summary
This summary is machine-generated.

Human galectins bind to bacterial polysaccharides, revealing new targets beyond typical sugar structures. This finding expands understanding of galectin interactions and potential antibacterial mechanisms.

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Area of Science:

  • Glycobiology
  • Immunology
  • Microbiology

Background:

  • Galectins are key regulators of cellular processes through protein-glycan interactions.
  • Certain galectins exhibit antibacterial properties by targeting histo-blood group epitopes.
  • The precise carbohydrate-binding specificities of galectins beyond β-galactosides remain incompletely understood.

Purpose of the Study:

  • To investigate whether carbohydrate determinants other than β-galactosides serve as binding sites for human galectins.
  • To explore the binding capabilities of human galectins-4, -8, and -9 to a diverse array of bacterial polysaccharides.
  • To assess the potential of a novel array-based screening tool for identifying galectin-carbohydrate interactions.

Main Methods:

  • Construction and utilization of an array containing various bacterial polysaccharides.
  • Testing the binding activity of human galectins (galectin-4, -8, -9) against the polysaccharide array.
  • Inclusion of positive controls (histo-blood group ABH-epitopes, E. coli 086 polysaccharide) to validate the experimental setup.

Main Results:

  • Significant galectin binding signals were detected, varying with specific galectin and polysaccharide combinations.
  • Binding was observed even for polysaccharides lacking typical β-galactoside structures, such as rhamnan.
  • The presence of β-galactoside-related epitopes did not guarantee binding, indicating complex recognition mechanisms.

Conclusions:

  • The developed array serves as a valuable tool for screening galectin-carbohydrate interactions.
  • Human galectins can bind to bacterial polysaccharides through determinants beyond β-galactosides.
  • These findings provide crucial direction for future functional and structural studies of galectin-mediated immunity and bacterial interactions.