Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin

Spik, Geneviève; Bayard, Bernard; Fournet, Bernard; Strecker, Gérard; Bouquelet, Stéphane; Montreuil, Jean

doi:10.1016/0014-5793(75)80513-8

Cited by 290 publications

(60 citation statements)

References 11 publications

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“…6C). As positive control for SNA binding human plasma transferrin was used that contains peripheral NeuAc·2,6-linked (35). Collectively, the results showed ovarian carcinoma cell type-specific glycosylation.…”

Section: Lectin-binding Properties Of Human Ovarian Carcinoma Cellsmentioning

confidence: 86%

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Escrevente

Machado²,

Brito³

et al. 2006

Int J Oncol

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Section: Lectin-binding Properties Of Human Ovarian Carcinoma Cellsmentioning

confidence: 86%

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Escrevente

Machado²,

Brito³

et al. 2006

Int J Oncol

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“…Five different charge isoforms can be identified by isoelectric focusing, which represent polypeptide chains containing from zero to four sialic acid residues (3,15). Transferrin is known to contain two N-linked glycosylation sites, consisting of 80% biantennary structures and 20% tri-and tetraantennary structures (33,34 (20,21). However, a subsequent study indicates that the defect is not the synthesis of dolichyl phosphate or N-acetylglucosaminyl-pyrophosphoryl-dolichol (35).…”

Section: Discussionmentioning

confidence: 99%

Carbohydrate-deficient glycoprotein syndrome: not an N-linked oligosaccharide processing defect, but an abnormality in lipid-linked oligosaccharide biosynthesis?

Powell¹,

Paneerselvam²,

Vij³

et al. 1994

J. Clin. Invest.

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The carbohydrate-deficient glycoprotein syndrome (CDGS) is a developmental disease associated with an abnormally high isoelectric point of serum transferrin. Carbohydrate analyses of this glycoprotein initially suggested a defect in N-linked oligosaccharide processing, although more recent studies indicate a defect in the attachment of these sugar chains to the protein. We studied both serum glycoproteins and fibroblast-derived [2-3H]mannose-labeled oligosaccharides from CDGS patients and normal controls. While there was a decrease in the glycosylation of serum glycoproteins of affected individuals, differences were not seen in either monosaccharide composition or oligosaccharide structures. The lectin-binding profiles of glycopeptides from [2-3H]-mannose-labeled fibroblasts were likewise indistinguishable. However, the incorporation of [2-3H]mannose into both glycoproteins and the dolichol-linked oligosaccharide precursor was significantly reduced. Thus, at least in some patients, CDGS is not due to a defect in processing of N-linked oligosaccharides, but rather to defective synthesis and transfer of nascent dolichol-linked oligosaccharide precursors. This abnormality could result in both a failure to glycosylate some sites on some proteins, as well as secondary abnormalities in overall glycoprotein processing and/or function. (J.

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“…AGP-A is a form of AGP that contains a reduced amount of biantennary chains (37a). Apo-transferrin is known to be glycosylated with two biantennary N-linked glycan chains that contain ␣2,6 terminal sialic acids linked to lactosamine (4,38). Fractions of glycans purified from AGP, AGP-A, and apo-transferrin can also be fucosylated to create the sLe X motif [NeuAc␣2-3/6Gal␤1-4(Fuc␣1-3)GlcNAc], which is a marker for cancer cells.…”

Section: Vol 80 2006 Sialic Acid Is Required For Aav1 and Aav6 Tranmentioning

confidence: 99%

α2,3 and α2,6 N-Linked Sialic Acids Facilitate Efficient Binding and Transduction by Adeno-Associated Virus Types 1 and 6

Miller

Agbandje‐McKenna

et al. 2006

J Virol

271

227

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Recombinant adeno-associated viruses (AAVs) are promising vectors in the field of gene therapy. Different AAV serotypes display distinct tissue tropism, believed to be related to the distribution of their receptors on target cells. Of the 11 well-characterized AAV serotypes, heparan sulfate proteoglycan and sialic acid have been suggested to be the attachment receptors for AAV type 2 and types 4 and 5, respectively. In this report, we identify the receptor for the two closely related serotypes, AAV1 and AAV6. First, we demonstrate using coinfection experiments and luciferase reporter analysis that AAV1 and AAV6 compete for similar receptors. Unlike heparin sulfate, enzymatic or genetic removal of sialic acid markedly reduced AAV1 and AAV6 binding and transduction. Further analysis using lectin staining and lectin competition assays identified that AAV1 and AAV6 use either ␣2,3-linked or ␣2,6-linked sialic acid when transducing numerous cell types (HepG2, Pro-5, and Cos-7). Treatment of cells with proteinase K but not glycolipid inhibitor reduced AAV1 and AAV6 infection, supporting the hypothesis that the sialic acid that facilitates infection is associated with glycoproteins rather than glycolipids. In addition, we determined by inhibitor (N-benzyl GalNAc)-and cell line-specific (Lec-1) studies that AAV1 and AAV6 require N-linked and not O-linked sialic acid. Furthermore, a resialylation experiment on a deficient Lec-2 cell line confirmed a 2,3 and 2,6 N-linked sialic acid requirement, while studies of mucin with O-linked sialic acid showed no inhibition effect for AAV1 and AAV6 transduction on Cos-7 cells. Finally, using a glycan array binding assay we determined that AAV1 efficiently binds to NeuAc␣2-3GalNAc␤1-4GlcNAc, as well as two glycoproteins with ␣2,3 and ␣2,6 N-linked sialic acids. Taken together, competition, genetic, inhibitor, enzymatic reconstitution, and glycan array experiments support ␣2,3 and ␣2,6 sialic acids that are present on N-linked glycoproteins as primary receptors for efficient AAV1 and AAV6 viral infection.Adeno-associated viruses (AAVs), dependoviruses of the parvovirus family, rely on a helper virus, such as adenovirus or herpesvirus, to complete their life cycle. In recent years, AAVs have become promising vectors for gene therapy, due to their nonpathogenicity and their ability to mediate long-term transgene expression. Among the 11 AAV serotypes (AAV1 to AAV11) and over 100 variants (12,24), AAV2 is the best characterized and the predominant serotype used in clinical trials. However, more and more studies suggest that AAV2-based vectors are rate limiting in certain tissues (5, 32). The availability of other AAV serotypes with tissue preference for transduction, such as AAV1 and AAV6 for muscle (2, 5) and AAV8 for liver (12,14,25), has overcome this restriction. The enhanced tropism of AAV serotypes in different organs is dictated by their capsid amino acid sequences and is believed in part to be related to the cumulative effects of viral binding to multiple cell surface receptors,...

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Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin

Cited by 290 publications

References 11 publications

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Carbohydrate-deficient glycoprotein syndrome: not an N-linked oligosaccharide processing defect, but an abnormality in lipid-linked oligosaccharide biosynthesis?

α2,3 and α2,6 N-Linked Sialic Acids Facilitate Efficient Binding and Transduction by Adeno-Associated Virus Types 1 and 6

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