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dc.contributor.authorIssa, Samah
dc.contributor.authorMoran, Anthony P
dc.contributor.authorUstinov, Sergey N
dc.contributor.authorLin, Jack Han-Hsing
dc.contributor.authorLigtenberg, Antoon J
dc.contributor.authorKarlsson, Niclas G
dc.date.accessioned2018-09-20T16:11:45Z
dc.date.available2018-09-20T16:11:45Z
dc.date.issued2010-04-29
dc.identifier.citationIssa, Samah; Moran, Anthony P; Ustinov, Sergey N; Lin, Jack Han-Hsing; Ligtenberg, Antoon J; Karlsson, Niclas G (2010). O-linked oligosaccharides from salivary agglutinin: helicobacter pylori binding sialyl-lewis x and lewis b are terminating moieties on hyperfucosylated oligo-n-acetyllactosamine. Glycobiology 20 (8), 1046-1057
dc.identifier.issn1460-2423,0959-6658
dc.identifier.urihttp://hdl.handle.net/10379/12049
dc.description.abstractSalivary agglutinin plays a vital biological role modulating the protective effect in the oral cavity by interacting with a broad range of oral pathogens. Here, we describe the first characterization of the O-linked oligosaccharides of salivary agglutinin identified by negative ion liquid chromatography-mass spectrometry. The dominating structures were neutral or monosialylated core 1 (Gal beta 1-3GalNAc alpha 1-Ser/Thr) and core 2 (Gal beta 1-3(GlcNAc beta 1-6)GalNAc alpha 1-Ser/Thr) structures extended by fucosylated oligo-N-acetyllactosamine units. Oligosaccharides detected as [M-H](-) or [M-2H](2-) ions ranged from the disaccharide Gal beta 1-3GalNAcol up to structures of almost 4000 Da, corresponding to core 1/2 structures with five N-acetyllactosamine units and 11 fucoses. Fucose was found either as terminal or internal blood group H structures in type 1 (Gal beta 1-3GlcNAc beta 1-R), type 2 (Gal beta 1-4GlcNAc beta 1-R) and type 3 (Gal beta 1-3GalNAc alpha 1-Ser/Thr) units, where the chains also could be fucosylated on GlcNAc yielding repeated Lewis a/b or Lewis x/y structures. Sialylation was located either at the non-reducing end of the N-acetyllactosamine chains as sialyl-Lewis x or as sialyl-T (NeuAc alpha 2-3Gal beta 1-3GalNAc alpha 1-Ser/Thr) type structures with or without further extension of the C-6 branch of GalNAc with neutral fucosylated N-acetyllactosamine chains. The data indicated that sialylation, fucosylation and type 1 N-acetyllactosamine termination are important regulatory elements for controlling the oligosaccharide chain length. Furthermore, it was shown that these regulatory oligosaccharide elements could be utilized by the pathogen Helicobacter pylori to colonize the oral cavity, reside in dental plaque and serve as a reservoir for reinfection after successful clearance of H. pylori gastric infection.
dc.publisherOxford University Press (OUP)
dc.relation.ispartofGlycobiology
dc.subjectblood group antigen binding adhesin
dc.subjectdeleted in malignant brain tumor 1
dc.subjectglycomics
dc.subjectmass spectrometry
dc.subjectsialic acid binding adhesin
dc.subjectcomplete genome sequence
dc.subjectrich protein gp-340
dc.subjectstreptococcus-mutans
dc.subjectblood-group
dc.subjectmucin-type
dc.subjectinfection
dc.subjectreceptor
dc.subjectglycoproteins
dc.subjectadhesion
dc.subjectstrain
dc.titleO-linked oligosaccharides from salivary agglutinin: helicobacter pylori binding sialyl-lewis x and lewis b are terminating moieties on hyperfucosylated oligo-n-acetyllactosamine
dc.typeArticle
dc.identifier.doi10.1093/glycob/cwq066
dc.local.publishedsourcehttps://academic.oup.com/glycob/article-pdf/20/8/1046/16653975/cwq066.pdf
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