Structural analysis of monosulfated side-chain oligosaccharides isolated from human tracheobronchial mucous glycoproteins

Mawhinney, Thomas P.; Adelstein, Edward H.; Gayer, Debra; Landrum, Deborah C.; Barbero, Giulio J.

doi:10.1016/0008-6215(92)80016-t

Cited by 36 publications

(16 citation statements)

References 30 publications

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“…In addition, there was a substantial increase in sulfated, sialylated, and fucosylated O-glycan structures, and over 260 compositionally different O-glycans were identified in the mucins by matrix-assisted laser/desorption ionization mass spectrometry (MALDI) [23] which is consistent with previous studies showing that airway mucins from CF patients have a high content of a variety of O-glycans containing sialylated, sulfated, and fucosylated glycans in addition to the sialyl-Le x epitope and its sulfated derivatives [45][46][47][48][49][50][51][52][53][54][55][56][57]. The high density presentation of sialyl-Le x epitope on CF mucins may be especially favorable for P. aeruginosa attachment and colonization within the lung space.…”

Section: Discussionsupporting

confidence: 88%

Pseudomonas aeruginosa mucoid strain 8830 binds glycans containing the sialyl-Lewis x epitope

2006

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Pseudomonas aeruginosa infection of patients with cystic fibrosis (CF) is a leading cause of their morbidity and mortality. Pathogenesis is initiated in part by molecular interactions of P. aeruginosa with carbohydrate residues in airway mucins that accumulate in the lungs of patients with this disease. To explore the nature of the glycans recognized by a stable, mucoid, alginate-producing strain P. aeruginosa 8830 we generated a genetically modified Pa8830 expressing green fluorescent protein (Pa3380-GFP). We tested its binding to a panel of glycolipids and neoglycolipids in which selected glycans were covalently attached to dipalmitoyl phosphatidylethanolamine and analyzed on silica gel surfaces. Among all glycans tested, Pa8830-GFP bound best to sialyl-Le(x)-containing glycan NeuAc(alpha2-3)Gal(beta1-4)[Fuc(alpha1-3)]GlcNAc-R and bound weakly to H-type blood group Fucalpha1-2Galbeta1-4GlcNAc-R, sialyl-lactose, and Le(x), and exhibited little binding toward non-fucosylated derivatives. Interestingly, while Pa8830-GFP bound to the glycosphingolipid asialoGM1, it did not appear to bind to a wide variety of other glycosphingolipids including GM1, GM2, asialoGM2, and sulfatide. These results indicate that P. aeruginosa 8830 has preferential binding to sialyl-Le(x)-containing glycans and has weak recognition of related fucose- and sialic acid-containing glycans. The finding that Pa8830 binds sialyl-Le(x)-containing glycans, which occur at increased levels in mucins from CF patients, is consistent with studies of other strains of P. aeruginosa and further suggests that such glycans on CF mucins contribute to disease pathogenesis.

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Section: Discussionsupporting

confidence: 88%

Pseudomonas aeruginosa mucoid strain 8830 binds glycans containing the sialyl-Lewis x epitope

2006

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“…Structural studies have shown that respiratory mucins are sulfated either on galactose or on N-acetylglucosamine (2)(3)(4)(5)(6), and it has been shown that respiratory epithelial cells in secondary culture were able to secrete sulfated mucins (7). Strong negative charges confer important biological functions on sulfated carbohydrate chains.…”

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confidence: 99%

Characterization of a Sulfotransferase from Human Airways Responsible for the 3-O-Sulfation of Terminal Galactose in N-Acetyllactosamine-containing Mucin Carbohydrate Chains

Lo-Guidice

Périni

Lafitte

et al. 1995

Journal of Biological Chemistry

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A galactose 3-O-sulfotransferase activity able to transfer a sulfate group from adenosine 3'-phosphate 5'-phosphosulfate to methyl galactosides or terminal N-acetyllactosamine-containing carbohydrate chains from human respiratory mucins was characterized in microsomal fractions prepared from human respiratory mucosa. The reaction products, methyl alpha- or beta-galactose 3-sulfate and three oligosaccharide alditols containing the sequence HSO3-3Gal beta 1-4GlcNAc beta 1-6GalNAc-itol were identified by high performance anion-exchange chromatography. Using methyl beta-galactoside as a substrate, the optimum activity was obtained with 0.1% Triton X-100, 30 mM NaF, 20 mM Mn2+, and 10 mM AMP in a 30 mM 2-(N-morpholino)ethanesulfonic acid buffer at pH 6.1. The apparent Km for methyl beta-galactoside and for adenosine 3'-phosphate 5'-phosphosulfate were observed at 0.69 x 10(-3) M and at 4 x 10(-6) M respectively. This sulfotransferase is different from that responsible for sulfatide synthesis.

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“…While tandem MS cannot precisely determine the position of the sulfate group, it has been previously reported that sulfate groups in mucins human are attached to C-3, C-4, or C-6 of a galactose or C-6 of N-acetylglucosamine. 41 It should be noted that in these tandem MS spectra, losses of the sulfate groups are not observed.…”

Section: Resultsmentioning

confidence: 76%

Characterization of Novel O-Glycans Isolated from Tear and Saliva of Ocular Rosacea Patients

Özcan¹,

An²,

Vieira

et al. 2013

J. Proteome Res.

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O-glycans in saliva and tear isolated from patients suffering from ocular rosacea, a form of inflammatory ocular surface disease, were profiled and their structures were elucidated using high resolution mass spectrometry. We have previously shown that certain structures, particularly sulfated oligosaccharides, increased in the tear and saliva of rosacea patients. In this study, the structures of these glycans were elucidated using primarily tandem mass spectrometry. There were important similarities in the glycan profiles of tears and saliva with the majority of the structures in common. The structures of the most abundant species common to both tear and saliva, which were also the most abundant species in both, were elucidated. For sulfated species, the positions of the sulfate groups were localized. The majority of the structures were new, with the sulfated glycans comprising of mucin core 1 and core 2-typestructures. As both saliva and tear are rich in mucins, it is suggested that the O-glycans are mainly components of mucins. The study further illustrates the strong correspondence between the glycans in the tear and saliva of ocular rosacea patients.

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Structural analysis of monosulfated side-chain oligosaccharides isolated from human tracheobronchial mucous glycoproteins

Cited by 36 publications

References 30 publications

Pseudomonas aeruginosa mucoid strain 8830 binds glycans containing the sialyl-Lewis x epitope

Pseudomonas aeruginosa mucoid strain 8830 binds glycans containing the sialyl-Lewis x epitope

Characterization of a Sulfotransferase from Human Airways Responsible for the 3-O-Sulfation of Terminal Galactose in N-Acetyllactosamine-containing Mucin Carbohydrate Chains

Characterization of Novel O-Glycans Isolated from Tear and Saliva of Ocular Rosacea Patients

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