Structural analysis of the carbohydrate moieties of human tamm-horsfall glycoprotein

Williams, Julie; Marshall, Ruth; Halbeek, Herman van; Vliegenthart, J.F.G.

doi:10.1016/0008-6215(84)85029-6

Cited by 54 publications

(22 citation statements)

References 34 publications

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“…1979;Soh et al, 1980;Afonso et al, 1981;Donald et al, 1982Donald et al, , 1983Williams et al, 1984;Serafini-Cessi et al, 1984a, b;Donald and Feeney, 1986;Dall'Olio et al, 1988;Smagula et al, 1990). Tn the present study the N-linked carbohydrates were enzymically released from T-H glycoprotein of one male donor by PNGase-F, and fractionated into more than 150 fractions by a combination of three liquidchromatographic techniques.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, the structure has been determined of a Sd" active pentasaccharide cleaved from T-H glycoprotein with endo-P-galactosidase (Donald et al, 1983;Donald and Feeney, 1986). Previous studies on T-H-glycopeptide mixtures have revealed that the Sd" determinant resides in the nonreducing termini of branched N-glycans (Williams et al, 1984). In addition to sialylated compounds, small amounts of oligomannose-type carbohydrates have been reported to occur in the glycoprotein (Afonso et al, 1981;Dall'Olio et al, 1988).…”

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confidence: 99%

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The Asn‐linked carbohydrate chains of human Tamm‐Horsfall glycoprotein of one male

Hård

Zadelhoff

Moonen

et al. 1992

European Journal of Biochemistry

277

154

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Human Tamm-Horsfall glycoprotein has been purified from the urine of one male. The Asn-linked carbohydrate chains were enzymically released by peptide-N4-(N-acetyl-~-glucosaminyl)asparagine amidase F, and separated from the remaining protein by gel-permeation chromatography on BioGel P-100. Fractionation of the intact (sulfated) sialylated carbohydrate chains was achieved by a combination of three liquid-chromatographic techniques, namely, anion-exchange FPLC on QSepharose, amine-adsorption HPLC on Lichrospher-NH2, and high-pH anion-exchange chromatography on CarboPac PA1. In total, more than 1 SO carbohydrate-containing fractions were obtained, some of which still contained mixtures of oligosaccharides. The primary structure of 30 N-glycans, including 10 novel oligosaccharides, were determined by one-and two-dimensional 'H-NMR spectroscopy at 500 MHz or 600 MHz. The types of compounds identified range from non-fucosylated, monosialylated, diantennary to fucosylated, tetrasialylated, tetraantennary carbohydrate chains, possessing the following terminal structural elements :NeuSAccl2 -3GalP1!-4GlcNAcPI - \ .The largest GalNAc-containing compound has the following structure : GalNAcPl

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

The Asn‐linked carbohydrate chains of human Tamm‐Horsfall glycoprotein of one male

Hård

Zadelhoff

Moonen

et al. 1992

European Journal of Biochemistry

277

154

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“…THP is known to be a heavily glycosylated protein, with carbohydrates accounting for 30% of the total molecular mass (55). About 80% of the carbohydrate moieties expressed on human THP are of the complex type, with sialylated tri-and tetraantennary structures (37). However, proteolytic digestion of human urinary THP consistently yielded high mannose-bearing glycopeptides.…”

Section: Tamm-horsfall Protein As a Major Urinary Defense Factormentioning

confidence: 99%

“…These studies were, however, not performed in the context of well defined E. coli strains or in the presence of the cognate urothelial receptors. It was also unclear whether THP possesses a single, well conserved, high-mannose chain that is necessary for type 1 fimbrial binding (37,38) and whether soluble urinary THP is capable of interacting at all with the fimbriae (35). There have also been questions regarding the specificity of the THP-E. coli interaction as non-mannose-specific P fimbriae were found to bind THP (39).…”

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confidence: 99%

Tamm-Horsfall Protein Binds to Type 1 Fimbriated Escherichia coli and Prevents E. coli from Binding to Uroplakin Ia and Ib Receptors

Pak

Pu²,

Zhang³

et al. 2001

Journal of Biological Chemistry

274

201

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The adherence of uropathogenic Escherichia coli to the urothelial surface, a critical first step in the pathogenesis of urinary tract infection (UTI), is controlled by three key elements: E. coli adhesins, host receptors, and host defense mechanisms. Although much has been learned about E. coli adhesins and their urothelial receptors, little is known about the role of host defense in the adherence process. Here we show that Tamm-Horsfall protein (THP) is the principal urinary protein that binds specifically to type 1 fimbriated E. coli, the main cause of UTI. The binding was highly specific and saturable and could be inhibited by D-mannose and abolished by endoglycosidase H treatment of THP, suggesting that the binding is mediated by the high-mannose moieties of THP. It is species-conserved, occurring in both human and mouse THPs. In addition, the binding to THP was much greater with an E. coli strain bearing a phenotypic variant of the type 1 fimbrial FimH adhesin characteristic of those prevalent in UTI isolates compared with the one prevalent in isolates from the large intestine of healthy individuals. Finally, a physiological concentration of THP completely abolished the binding of type 1 fimbriated E. coli to uroplakins Ia and Ib, two putative urothelial receptors for type 1 fimbriae. These results establish, on a functional level, that THP contains conserved high-mannose moieties capable of specific interaction with type 1 fimbriae and strongly suggest that this major urinary glycoprotein is a key urinary anti-adherence factor serving to prevent type 1 fimbriated E. coli from binding to the urothelial receptors.The adhesion of Escherichia coli, the most common cause of urinary tract infection (UTI), 1 to urothelial cells is a crucially important first step in UTI pathogenesis (1-5). This adhesion process frequently requires filamentous surface appendages of uropathogenic E. coli that are called fimbriae, or pili. Epidemiological studies have shown that Ͼ90% of all E. coli isolates from UTI patients elaborate type 1 fimbriae (also named mannose-sensitive fimbriae) (4, 6, 7). Although controversies existed for several years, recent investigations have unequivocally documented the importance of type 1 fimbriae as a major urovirulence factor. For instance, of the nine most common E. coli virulence factors, the genes for type 1 fimbriae emerged as the only trait common in all 203 UTI isolates examined (8). In addition, 26% of the 203 strains were positive only for type 1 fimbrial genes and were negative for the eight other urovirulence factors tested, including P, S, and Dr fimbriae. In experimental mouse models, type 1 fimbriae were shown to be indispensable for bladder colonization and infection (9). Conversely, systemic immunization of mice with the FimH tip adhesin of type 1 fimbriae reduced bladder colonization of E. coli by 99% even in neutropenic mice, suggesting that blocking type 1 fimbriae could completely abolish E. coli adhesion (10). Further evidence supporting an important role of type 1 fimbriae ...

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“…Furthermore, GalNAc H1 is observed at δ 4.73Ϫ4.76 (42°C), while its NAc signal resonates at δ 2.015Ϫ2.019. Due to the attachment of GalNAc to Gal via a (β1-4) linkage, Gal H4 resonates at δ 4.11Ϫ4.12 and H3 at δ 4.15 (Williams et al, 1984;Donald and Feeney, 1986;Hård et al, 1992).…”

Section: Generalmentioning

confidence: 99%

Sulfated di‐, tri‐ and tetraantennary N‐glycans in human Tamm‐Horsfall glycoprotein

Rooijen

Kamerling

Vliegenthart

1998

European Journal of Biochemistry

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The primary structures of 32 sulfated di-, tri-and tetraantennary N-glycans of human Tamm-Horsfall glycoprotein (THP) have been determined. THP was isolated from the urine of one healthy male donor. The intact carbohydrate chains were released by PNGase-F and fractionated via FPLC on Resource Q, HPLC on LiChrosorb-NH 2 , and high-pH anion-exchange chromatography on CarboPac PA-1. Characterizations were performed using 500-MHz and 600-MHz 1 H-NMR spectroscopy, in combination with sialidase treatments. The type of characterized N-glycans ranged from monosulfated to trisulfated N-glycans, whereby the sulfate groups were present as 3-O-sulfated Gal (Gal3S) and 4-O-sulfated GalNAc (GalNAc4S). A compilation of the established structures is shown below.

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Structural analysis of the carbohydrate moieties of human tamm-horsfall glycoprotein

Cited by 54 publications

References 34 publications

The Asn‐linked carbohydrate chains of human Tamm‐Horsfall glycoprotein of one male

The Asn‐linked carbohydrate chains of human Tamm‐Horsfall glycoprotein of one male

Tamm-Horsfall Protein Binds to Type 1 Fimbriated Escherichia coli and Prevents E. coli from Binding to Uroplakin Ia and Ib Receptors

Sulfated di‐, tri‐ and tetraantennary N‐glycans in human Tamm‐Horsfall glycoprotein

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