Structural characterization of neutral oligosaccharides with blood-group A and H activity isolated from bovine submaxillary mucin

Savage, Angela V.; D'Arcy, Sinéad; Donoghue, Carmel M.

doi:10.1042/bj2790095

Cited by 18 publications

(9 citation statements)

References 22 publications

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“…Besides the species-specific expression of the αGal antigen on bovine digestive epithelial cells, another species-specific bovine characteristic was evidenced with regard to HBGAs expression. Indeed, we failed to detect HBGAs based on type 1 precursor (Galβ3GlcNAc) in bovine tissues or saliva, consistent with the results from earlier structural analyses of O-linked oligosaccharides from bovine salivary mucins which described the presence of type 2-based structures only [34],[35]. Those studies also failed to detect the αGal epitope.…”

Section: Discussionsupporting

confidence: 92%

The αGal Epitope of the Histo-Blood Group Antigen Family Is a Ligand for Bovine Norovirus Newbury2 Expected to Prevent Cross-Species Transmission

et al. 2009

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Among Caliciviridae, the norovirus genus encompasses enteric viruses that infect humans as well as several animal species, causing gastroenteritis. Porcine strains are classified together with human strains within genogroup II, whilst bovine norovirus strains represent genogroup III. Various GI and GII human strains bind to carbohydrates of the histo-blood group family which may be shared among mammalian species. Genetic relatedness of human and animal strains as well as the presence of potentially shared ligands raises the possibility of norovirus cross-species transmission. In the present study, we identified a carbohydrate ligand for the prototype bovine norovirus strain Bo/Newbury2/76/UK (NB2). Attachment of virus-like particles (VLPs) of the NB2 strain to bovine gut tissue sections showed a complete match with the staining by reagents recognizing the Galα1,3 motif. Alpha-galactosidase treatment confirmed involvement of a terminal alpha-linked galactose. Specific binding of VLPs to the αGal epitope (Galα3Galβ4GlcNAcβ-R) was observed. The binding of Galα3GalαOMe to rNB2 VLPs was characterized at atomic resolution employing saturation transfer difference (STD) NMR experiments. Transfection of human cells with an α1,3galactosyltransferase cDNA allowed binding of NB2 VLPs, whilst inversely, attachment to porcine vascular endothelial cells was lost when the cells originated from an α1,3galactosyltransferase KO animal. The αGal epitope is expressed in all mammalian species with the exception of the Hominidaea family due to the inactivation of the α1,3galactosyltransferase gene (GGTA1). Accordingly, the NB2 carbohydrate ligand is absent from human tissues. Although expressed on porcine vascular endothelial cells, we observed that unlike in cows, it is not present on gut epithelial cells, suggesting that neither man nor pig could be infected by the NB2 bovine strain.

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Section: Discussionsupporting

confidence: 92%

The αGal Epitope of the Histo-Blood Group Antigen Family Is a Ligand for Bovine Norovirus Newbury2 Expected to Prevent Cross-Species Transmission

et al. 2009

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“…Tn (GalNAcα1‐Ser/Thr) and T (Galβ(1–3)GalNAcα1‐Ser/Thr) antigens are also present in the porcine stomach mucin (Van Halbeek et al 1982; Zenteno et al 1995; Karlsson et al 1997). The bovine submaxillary mucin is a glycoprotein bearing at least 16 different structures (Savage et al 1990, 1991; Chai et al 1992). Of its oligosaccharides, 85% are acidic Olinked oligosaccharide chains, including a high density of sialyl Tn antigens and sialyl core 3 saccharide sequences (Table 2).…”

Section: Resultsmentioning

confidence: 99%

HCA and HML isolated from the red marine algae Hypnea cervicornis and Hypnea musciformis define a novel lectin family

et al. 2005

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HCA and HML represent lectins isolated from the red marine algae Hypnea cervicornis and Hypnea musciformis, respectively. Hemagglutination inhibition assays suggest that HML binds GalNAc/Gal substituted with a neutral sugar through 1-3, 1-4, or 1-2 linkages in O-linked mucin-type glycans, and Fuc(a1-6)GlcNAc of N-linked glycoproteins. The specificity of HCA includes the epitopes recognized by HML, although the glycoproteins inhibited distinctly HML and HCA. The agglutinating activity of HCA was inhibited by GalNAc, highlighting the different fine sugar epitope-recognizing specificity of each algal lectin. The primary structures of HCA (9193 6 3 Da) and HML (9357 6 1 Da) were determined by Edman degradation and tandem mass spectrometry of the N-terminally blocked fragments. Both lectins consist of a mixture of a 90-residue polypeptide containing seven intrachain disulfide bonds and two disulfide-bonded subunits generated by cleavage at the bond T 50 -E 51 (HCA) and R 50-E 51 (HML). The amino acid sequences of HCA and HML display 55% sequence identity (80% similarity) between themselves, but do not show discernible sequence and cysteine spacing pattern similarities with any other known protein structure, indicating that HCA and HML belong to a novel lectin family. Alignment of the amino acid sequence of the two lectins revealed the existence of internal domain duplication, with residues 1-47 and 48-90 corresponding to the N-and C-terminal domains, respectively. The six conserved cysteines in each domain may form three intrachain cysteine linkages, and the unique cysteine residues of the N-terminal (Cys46) and the C-terminal (Cys71) domains may form an intersubunit disulfide bond.

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“…Several groups have studied the O ‐glycans cleaved from bovine submaxillary mucin using various analytical techniques 25–32. Interestingly, all of the studied oligosaccharide pools were obtained by the traditional β‐elimination procedure.…”

Section: Resultsmentioning

confidence: 99%

Matrix‐assisted laser desorption/ionization mass spectrometry compatible β‐elimination of O‐linked oligosaccharides

Huang

Konse

Mechref

et al. 2002

Rapid Comm Mass Spectrometry

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A new beta-elimination procedure has been introduced to cleave O-linked oligosaccharides from low- to sub-microgram amounts of glycoproteins prior to analysis by mass spectrometry. Borane-ammonia complex in aqueous ammonia is used as a cleaving solution alternative to the sodium borohydride/sodium hydroxide medium conventionally used in beta-elimination. The procedure results in minimum sample purification, leading to minimal sample loss and consequently an overall enhancement in sensitivity. It was applied successfully in the analysis of bovine fetuin and submaxillary mucin, as well as to a complex bile-salt-stimulated lipase glycoprotein isolated from human milk.

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Structural characterization of neutral oligosaccharides with blood-group A and H activity isolated from bovine submaxillary mucin

Cited by 18 publications

References 22 publications

The αGal Epitope of the Histo-Blood Group Antigen Family Is a Ligand for Bovine Norovirus Newbury2 Expected to Prevent Cross-Species Transmission

The αGal Epitope of the Histo-Blood Group Antigen Family Is a Ligand for Bovine Norovirus Newbury2 Expected to Prevent Cross-Species Transmission

HCA and HML isolated from the red marine algae Hypnea cervicornis and Hypnea musciformis define a novel lectin family

Matrix‐assisted laser desorption/ionization mass spectrometry compatible β‐elimination of O‐linked oligosaccharides

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