Carbohydrate chains from human bronchial mucus glycoproteins: a wide spectrum of oligosaccharide structures

Lamblin, Geneviève; Lhermitte, Michel; Klein, André; Roussel, P; Halbeek, H. van; Vliegenthart, Johannes F.G.

doi:10.1042/bst0120599

Cited by 31 publications

(14 citation statements)

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“…The detection of ␣2-6-linked Sias on the upper airway epithelial brush border of humans (17) is consistent with all of the above information as is the presence of ␣2-6-linked Sias on the upper airway epithelium of ferrets (the only effective mammalian model for human influenza infection) (18). An additional reason for human influenza susceptibility lies in the selective expression of ␣2-3-linked Sias in the goblet cells that secrete mucins into the human upper airway lumen (17,19). These soluble mucins are unable to adsorb out the ␣2-6-Sia binding human viruses before they reach and infect the airway epithelial cells.…”

supporting

confidence: 60%

Human-specific Regulation of α2–6-linked Sialic Acids

Gagneux

Cheriyan

Hurtado-Ziola

et al. 2003

Journal of Biological Chemistry

171

148

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Many microbial pathogens and toxins recognize animal cells via cell surface sialic acids (Sias) that are ␣2-3-or ␣2-8-linked to the underlying glycan chain. Human influenza A/B viruses are unusual in preferring ␣2-6-linked Sias, undergoing a switch from ␣2-3 linkage preference during adaptation from animals to humans. This correlates with the expression of ␣2-6-linked Sias on ciliated human airway epithelial target cells and of ␣2-3-linked Sias on secreted soluble airway mucins, which are unable to inhibit virus binding. Given several known differences in Sia biology between humans and apes, we asked whether this pattern of airway epithelial Sia linkages is also human-specific. Indeed, we show that since the last common ancestor with apes, humans underwent a concerted bidirectional switch in ␣2-6-linked Sia expression between airway epithelial cell surfaces and secreted mucins. This can explain why the chimpanzee appears relatively resistant to experimental infection with human Influenza viruses. Other tissues showed additional examples of human-specific increases or decreases in ␣2-6-linked Sia expression and only one example of a change specific to certain great apes. Furthermore, while human and great ape leukocytes both express ␣2-6-linked Sias, only human erythrocytes have markedly up-regulated expression. These cell type-specific changes in ␣2-6-Sia expression during human evolution represent another example of a human-specific change in Sia biology. Because the data set involves multiple great apes, we can also conclude that Sia linkage expression patterns can be conserved during millions of years of evolution within some vertebrate taxa while undergoing sudden major changes in other closely related ones.

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supporting

confidence: 60%

Human-specific Regulation of α2–6-linked Sialic Acids

Gagneux

Cheriyan

Hurtado-Ziola

et al. 2003

Journal of Biological Chemistry

171

148

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“…Firstly, 5T4 appears to have few 0-linked carbohydrate structures; by comparison, up to 50%-95% of the mucin carbohydrate is bound by 0-linkages (Bramwell et al, 1983;Shimizu and Yamauchi, 1982). Digestion with endo-p-galactosidase reduces the molecular size of some mucins (Lamblin et al, 1984), but does not significantly alter the molecular size of 5T4. Finally, although mucins from a restricted number of cell lines show a molecular weight similar to that of 5T4, they demonstrate marked heterogeneity in molecular weight.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of 5T4, a tumour‐associated antigen

Hole¹,

Stern²

1990

Intl Journal of Cancer

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The monoclonal antibody (MAb) 5T4 defines a human trophoblast antigen marker with a restricted pattern of expression in normal adult tissues but this antigen is expressed on a variety of carcinomas. The purification of 5T4 antigenic molecules is described from term syncytiotrophoblast by a combination of lectin- and immunoaffinity chromatography and gel filtration giving up to 10,000-fold purification with 70% yield. The antigen is carried by non-associated glycoprotein molecules with an apparent molecular weight of 72 kDa on SDS-PAGE and a neutral pI. Removal of N-linked sugars by N-glycanase reveals a core protein of 42 kDa. Treatment with enzymes that cleave O-linked sugars does not substantially alter the molecular size. The native 5T4 molecules are very resistant to proteolysis until the N-linked sugars are removed or the glycoprotein is denatured and reduced. Glycopeptides generated by these approaches will be suitable for amino acid sequencing.

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“…An interpretation of the results obtained with the glycosidases is that the region with the highest molecular mass contains protein with both potential N-glycosylation sites occupied, whereas the middle region has one N-glycosylation site occupied and the lower region has no N-glycosylation. Digestion of the neuraminidasetreated CHO-hGM-CSF with an enzyme that removes 0-linked oligosaccharides (19) lowered the position of all three major bands, indicating the possibility of O-glycosylation (P.M., unpublished data). Effects of Deglycosylation on Immuno-and Bioreactivity.…”

Section: Methodsmentioning

confidence: 99%

Increased biological activity of deglycosylated recombinant human granulocyte/macrophage colony-stimulating factor produced by yeast or animal cells.

Moonen¹,

Mermod²,

Ernst³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

115

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Human granulocyte/macrophage colonystimulating factor (hGM-CSF) produced by several recombinant sources including Escherichia coli, yeast, and animal cells was studied. Recombinant animal cells produced hGM-CSF in low quantities and in multiple forms of varying size. Mammalian hGM-CSF was purified 200,000-fold using immunoaffnity and lectin chromatography. Partially purified proteins produced in yeast and mammalian cells were assayed for the effects of deglycosylation. Following enzymatic deglycosylation, immunoreactivity was measured by radiounmunoassay and biological activity was measured in vitro on responsive human primary cells. Removal of N-linked oligosaccharides from both proteins increased their immunoreactivities by 4-to 8-fold. Removal of these oligosaccharides also increased their specific biological activities about 20-fold, to reach approximately the specific activity of recombinant hGM-CSF from E. coil. The E.coli produced-protein-lacking any carbohydrate-had by far the highest specific activity observed for the recombinant hGM-CSFs.

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Carbohydrate chains from human bronchial mucus glycoproteins: a wide spectrum of oligosaccharide structures

Cited by 31 publications

References 0 publications

Human-specific Regulation of α2–6-linked Sialic Acids

Human-specific Regulation of α2–6-linked Sialic Acids

Isolation and characterization of 5T4, a tumour‐associated antigen

Increased biological activity of deglycosylated recombinant human granulocyte/macrophage colony-stimulating factor produced by yeast or animal cells.

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