Carbohydrate structures of bovine submaxillary mucin

Tsuji, Tsutomu; Osawa, Toshiaki

doi:10.1016/s0008-6215(00)90358-6

Cited by 115 publications

(61 citation statements)

References 33 publications

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“…S7C). Although the structure of the Tn-antigen BT4244_m complex suggests the protein cannot accommodate a modification on the O6 of the GalNAc residue, it provides little insight into the apparent inability of this protein to recognize the T-antigen; however, its seemingly strict requirement for the Tn-antigen likely explains the qualitatively limited activity of BT4244_m on BSM and fetuin, where the Tn-antigen is comparatively rare or nonexistent, respectively (19,20).…”

Section: Resultsmentioning

confidence: 99%

Recognition of protein-linked glycans as a determinant of peptidase activity

Noach

Ficko-Blean

Pluvinage

et al. 2017

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

137

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The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Earth, the fundamental details of how peptidases accommodate posttranslational modifications, including glycosylation, has not been addressed. Through biochemical analyses and X-ray crystallographic structures we show that to hydrolyze their substrates, three structurally related metallopeptidases require the specific recognition of O-linked glycan modifications via carbohydrate-specific subsites immediately adjacent to their peptidase catalytic machinery. The three peptidases showed selectivity for different glycans, revealing protein-specific adaptations to particular glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated residue. This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular understanding of glycoprotein degradation.

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Section: Resultsmentioning

confidence: 99%

Recognition of protein-linked glycans as a determinant of peptidase activity

Noach

Ficko-Blean

Pluvinage

et al. 2017

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

137

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“…Similar results were obtained by another experimental approach published by Rogers et al [4], showing that influenza C virus can agglutinate sialidase-treated erythrocytes, which were resialylated with Neu5,9Ac2 in ct(2,3) or a(2,6) linkage to the penultimate sugar. Since the latter type of linkage prevails in BSM [43] and this mucin strongly interacts with influenza C virus, it can be assumed that a(2,6)-linked Neu5,9Ac2 or Neu9AcSGc-residues [22] are responsible for virus binding (cf. Table 2).…”

Section: Discussionmentioning

confidence: 99%

Use of influenza C virus for detection of 9‐O‐acetylated sialic acids on immobilized glycoconjugates by esterase activity

Zimmer¹,

Reuter²,

Schauer³

1992

European Journal of Biochemistry

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An overlay and a solid-phase assay are presented which allow the specific detection of 9-0-acetylated sialic acids on sialoglycoconjugates immobilized on microtiter plates, nitrocellulose or separated on thin-layer chromatograms. The assay takes advantage of two different biological properties of influenza C virus, its high-affinity binding to 9-0-acetylated sialic acids and its sialate 9-0-acetylesterase that is used for detection of bound virus with fluorogenic or chromogenic substrates. Though simple and rapid, the assay is highly sensitive with a detection limit of 65 fmol9-0-acetylated sialic acid in 9-0-acetylated ganglioside GDla.Influenza C virus is able to bind to a wide spectrum of sialoglycoconjugates like mucins, serum glycoproteins or gangliosides containing naturally or synthetically 0-acetylated sialic acids. 9-0-Acetyl-N-glycoloylneuraminic acid can also function as a high-affinity receptor determinant for influenza C virus. While the acetyl ester at the 9 position is essential for virus binding in all cases, a 4-0-acetyl group is not recognized. In addition to a(2,3) or a(2,6) bonds, 9-0-acetyl-N-acetylneuraminic acid in a(2,8) linkage to N-acetylneuraminic acid is also functionally active.Sialic acids are a Family of about 30 related sugars derived from neuraminic acid, which is the most diversely substituted sugar known in nature. This diversity mainly arises from acetylations that can take place at positions 4,7. 8, and/or 9. In most cases sialic acids occupy the terminal positions of glycoconjugates. Thcir involvement in many biological phenomena, especially as regulation of molecular and cellular recognition is concerned, has been well established [l]. In recent years, the interest in 0-acetylated sialic acids has rapidly increased, since some biological properties of these sugars seem to be associated with these modifications. Examples are the partial or complete block of sialidase action [2,3], binding of influenza C viruses and coronaviruses to cells [4, 51, antigenicity of bacterial capsules [6], modulation of the alternative pathway of complement activation [7], the expression of Nacetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) [8] as a differentiation marker on chicken erythrocytes [9], the association of 9-0-acetylated gangliosides with cell migration in rat brain development [lo], and the expression of an 0-acetylated Correspondence to R. Schauer, Biochemisches Institut, ChristianAlbrechts-Universitat, Okhausenslrasse 40, W-2300 Kiel, Federal Republic of Germany Abbreviution?. RSM, bovine submandibular gland mucin; DMB, 1,2-diamino-4,5-methylenedioxybenzene; ESM, equine submandibular gland mucin; GalNAc, N-acetylgalactosamine; Lac-Cer, lactosylceramide; McUmbAc, 4-methylumbelliferyl acetatc; Neu4,5Ac2, Nacetyl-4-O-acetylneuraminic acid; Neu4AcSGc. N-glycoloyl-4-O-acetylneuraminic acid; Neu5Ac, N-acctylneuraminic acid; Neu5,7Ac2, N-acetyl-7-0-acetylneuraminic acid; Neu5,9Ac2, N-acetyl-9-Oacetylneuraminic acid; NeuSAcgLt, N-acetyl-9-0-lactoylneuraminic acid; Neu9AcSGc, N-glycoloyl-9-0-ac...

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“…This preparation (48 ng), corresponding to 60 pmol of GalNAc (37), was mixed with a purified preparation of linkage region hexasaccharide peptides (30 pmol as hexasaccharides) prepared by chondroitinase ABC digestion of peptide CS-A from whale cartilage (27), dried, and treated with 50 l of 0.5 M LiOH at 4°C for 18 h. The mixture was neutralized with acetic acid, and the sample was treated with anion-exchange resin AG 50W-X2 (H ϩ form). The unbound fraction was neutralized with 1 M NH 4 HCO 3 and was derivatized with 2AB as described above (30).…”

Section: Hplc Analysis Of the 2ab-derivatives Of The Linkage Region Omentioning

confidence: 99%

Determination of the Glycosaminoglycan-Protein Linkage Region Oligosaccharide Structures of Proteoglycans from Drosophila melanogaster and Caenorhabditis elegans

Yamada

Okada

Ueno

et al. 2002

Journal of Biological Chemistry

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Caenorhabditis elegans and Drosophila melanogaster are relevant models for studying the roles of glycosaminoglycans (GAG) during the development of multicellular organisms. The genome projects of these organisms have revealed the existence of multiple genes related to GAG-synthesizing enzymes. Although the putative genes encoding the enzymes that synthesize the GAG-protein linkage region have also been identified, there is no direct evidence that the GAG chains bind covalently to core proteins. This study aimed to clarify whether GAG chains in these organisms are linked to core proteins through the conventional linkage region tetrasaccharide sequence found in vertebrates and whether modifications by phosphorylation and sulfation reported for vertebrates are present also in invertebrates. The linkage region oligosaccharides were isolated from C. elegans chondroitin in addition to D. melanogaster heparan and chondroitin sulfate after digestion with the respective bacterial eliminases and were then derivatized with a fluorophore 2-aminobenzamide. Their structures were characterized by gel filtration and anion-exchange high performance liquid chromatography in conjunction with enzymatic digestion and matrix-assisted laser desorption ionization time-of-flight spectrometry, which demonstrated a uniform linkage tetrasaccharide structure of -GlcUA-Gal-Gal-Xyl-or -GlcUA-Gal-Gal-Xyl(2-O-phosphate)-for C. elegans chondroitin and D. melanogaster CS, respectively. In contrast, the unmodified and phosphorylated counterparts were demonstrated in heparan sulfate of adult flies at a molar ratio of 73:27, and in that of the immortalized D. melanogaster S2 cell line at a molar ratio of 7:93, which suggests that the linkage region in the fruit fly first becomes phosphorylated uniformly on the Xyl residue and then dephosphorylated. It has been established here that GAG chains in both C. elegans and D. melanogaster are synthesized on the core protein through the ubiquitous linkage region tetrasaccharide sequence, suggesting that indispensable functions of the linkage region in the GAG synthesis have been well conserved during evolution. Mutations affecting the genes encoding putative proteins related to GAG biosynthetic enzymes have also been described for these organisms. Mutations in the tout velu (ttv) gene of D. melanogaster cause defects in Hedgehog movement in mosaic wing discs (1, 6). The ttv gene is a putative ortholog of vertebrate EXT1, which encodes a heparan polymerase and is associated with the hereditary multiple exostoses syndrome in humans (7). The pipe gene, which affects dorsal-ventral patterning of D. melanogaster development, encodes a homolog of vertebrate HS 2-O-sulfotransferase (2, 8). The sugarless and sulfateless genes, both of which affect the fibroblast growth factor signaling during the D. melanogaster development, en-

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Carbohydrate structures of bovine submaxillary mucin

Cited by 115 publications

References 33 publications

Recognition of protein-linked glycans as a determinant of peptidase activity

Recognition of protein-linked glycans as a determinant of peptidase activity

Use of influenza C virus for detection of 9‐O‐acetylated sialic acids on immobilized glycoconjugates by esterase activity

Determination of the Glycosaminoglycan-Protein Linkage Region Oligosaccharide Structures of Proteoglycans from Drosophila melanogaster and Caenorhabditis elegans

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