Structural diversity and biological importance of ABO, H, Lewis and secretor histo-blood group carbohydrates

Mattos, Luiz Carlos de

doi:10.1016/j.bjhh.2016.07.005

Cited by 56 publications

(58 citation statements)

References 60 publications

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“…HBGAs are synthesized by sequential addition of a carbohydrate moiety to a precursor disaccharide in successive steps that are genetically controlled by ABO (ABO, 9q34.1), H (FUT1, 19q13.3), secretor (FUT2, 19q13. 3) and Lewis (FUT3, 19p13.3 ) gene families [24]. For example, the FUT2 gene encodes an α-1,2fucosyltransferase that catalyzes addition of an α-1,2-fucose to the precursor oligosaccharides, forming H-type antigens, while the FUT3 gene encodes an α-1,3/4-fucosyltransferase that turns precursor oligosaccharides or H-type antigens into Le a or Le b antigens.…”

Section: Introductionmentioning

confidence: 99%

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Yang

Tan

et al. 2019

Preprint

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Initial cell attachment of rotavirus (RV) to specific cell surface glycans, which is the essential first step in RV infection, is mediated by the VP8* domain of the spike protein VP4. Recently, human histo-blood group antigens (HBGAs) have been identified as ligands or receptors for human RV strains. RV strains in the P[4] and P[8] genotypes of the P[II] genogroup share common recognition of the Lewis b and H type 1 antigens, while P[6], which is one of the other genotypes in P[II], only recognizes the H type 1 antigen. The molecular basis of receptor recognition by the major human P[8] RVs remains unknown due to lack of experimental structural information. Here, we used nuclear magnetic resonance (NMR) titration experiments and NMRderived high ambiguity driven docking (HADDOCK) methods to elucidate the molecular basis for P[8] VP8* recognition of the Le b and type 1 HBGAs and for P[6] recognition of H type 1 HBGAs. Unlike P[6] VP8* that recognizes H type 1 HGBAs in a binding surface composed of an α-helix and a β-sheet, referred as "βα binding domain", the P[8] VP8* binds the type 1 HBGAs requiring the presence of the Lewis epitope in a previously undescribed pocket formed by two β-sheets, referred as "β binding domain". The observation that P[6] and P[8] VP8* domains recognize different glycan structures at distinct binding sites supports the hypothesis that RV evolution is driven, at least in part, by selective pressure driven adaptation to HBGA structural diversity of their natural hosts living in the world. Recognition of the role that HBGAs play in driving RV evolution is essential to understanding RV diversity, host ranges, disease burden and zoonosis and to developing strategies to improve vaccines against RV infections.

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Section: Introductionmentioning

confidence: 99%

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Yang

Tan

et al. 2019

Preprint

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“…Type II disaccharide Galβ4GlcNAcβOR ( 3 ) 30 and its 6- O -sulfated analog Galβ4GlcNAc6SβOR ( 4 ) 32 were also excellent acceptors for α1– 3-fucosylation by Hp3/4FT to produce Galβ4(Fucα3)GlcNAcβProN 3 ( 13 , Le x antigen) and Galβ4(Fucα3)GlcNAc6SβProN 3 ( 14 ) in 98% and 93% yields, respectively. Mono-fucosylation of Type VI disaccharide Galβ4GlcβOR ( 5 ) 33-35 and lactose ( 6 ) led to the formation of Galβ4(Fucα3)GlcβProN 3 ( 15 ) and 3-fucosyllactose [ 16 , 3-FL, Galβ4(Fucα3)Glc] in 92% and 90% yields, respectively. 3-FL is one of the most abundant fucosylated HMOS that could inhibit bacterial or viral adhesion to human epithelial cells.…”

mentioning

confidence: 99%

H. pylori α1–3/4-fucosyltransferase (Hp3/4FT)-catalyzed one-pot multienzyme (OPME) synthesis of Lewis antigens and human milk fucosides

et al. 2017

Chem. Commun.

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Helicobacter pylori α1–3/4-fucosyltransferase (Hp3/4FT) was expressed in Escherichia coli at a level of 30 mg/L culture and used as a diverse catalyst in a one-pot multienzyme (OPME) system for high-yield production of L-fucose-containing carbohydrates including Lewis antigens such as Lewis a, b, x, O-sulfated Lewis x, and sialyl Lewis x as well as human milk fucosides such as 3-fucosyllactose (3-FL), lacto-N-fucopentaose (LNFP) III, lacto-N-difuco-hexaose (LNDFH) II and III. Noticeably, while difucosylation of tetrasaccharides was readily achieved using an excess amount of donor, synthesis of LNFP III was achieved by Hp3/4FT-catalyzed selective fucosylation of the N-acetyllactoamine (LacNAc) component in lacto-N-neotetraose (LNnT).

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“…The secretor gene encodes for α1,2 fucosyltransferase (FUT2), whereas the Lewis blood type is determined by the Lewis gene, which encodes for α1,3/1,4 fucosyltransferase (FUT3) (De Vries, Knegtel, Holmes, & Macher, ). Due to variations in the maternal fucosyltransferases the quantity and type of carbohydrates are differently expressed in pyloric or duodenal mucus and intestinal secretions (Mattos, ). Although HMOs and HMGPs fucosylation has been extensively studied (Doherty, Lodge, Dharmage, Dai, & Lowe, ), HMOs and HMGPs sialylation is not well understood yet (Grabarics, Csernák, Balogh, & Béni, ; Yan et al., ).…”

Section: Pre‐ and Postnatal Events Involved In Intestinal Barrier Matmentioning

confidence: 99%

Relationship Between Oligosaccharides and Glycoconjugates Content in Human Milk and the Development of the Gut Barrier

Figueroa-Lozano

Vos

2018

Comp Rev Food Sci Food Safe

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The intestinal immune barrier is considered to be the gatekeeper of the human body and rapidly develops directly after birth. Many pre‐ and postnatal factors influence the development of the gut‐barrier, which is composed of the microbiota, the mucus, the epithelial layer and the mucosal immune system. Even minor disturbances during barrier development can have consequences for health far into adulthood. Here we critically discuss the current knowledge on which pre‐ and postnatal factors influence development, maturation, and maintenance of the gut immune barrier. Human milk has a unique composition and is the gold standard for adequate development of the intestinal immune barrier. Not only the influence of human milk oligosaccharides (HMOs) but also that of glycoproteins (HMGPs) is reviewed. We discuss the influence of maternal genetic factors, such as the secretor and Lewis phenotypes on breast milk fucosylation and sialylation of HMOs and HMGPs. This diversity in HMOs and HMPGs influences microbiota composition and also the development of the immune barrier. Cow milk‐derived infant formula is often being used as an alternative for human breast milk. The consequences of this for proper development of the intestinal immune barrier and, in particular, the differences in the type of oligosaccharides and glycosylation patterns (sialic and fucose composition) between cow and human milk are critically discussed. Current and prospective strategies to promote proper gut‐immune maturation are proposed. These might include more personalized infant formulas when breast milk is not an option.

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Structural diversity and biological importance of ABO, H, Lewis and secretor histo-blood group carbohydrates

Cited by 56 publications

References 60 publications

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

H. pylori α1–3/4-fucosyltransferase (Hp3/4FT)-catalyzed one-pot multienzyme (OPME) synthesis of Lewis antigens and human milk fucosides

Relationship Between Oligosaccharides and Glycoconjugates Content in Human Milk and the Development of the Gut Barrier

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