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Review
. 2016 Aug;1860(8):1596-607.
doi: 10.1016/j.bbagen.2015.12.026. Epub 2015 Dec 31.

Histo-blood group glycans in the context of personalized medicine

Viktoria Dotz  1 , Manfred Wuhrer  2
Affiliations
Review

Histo-blood group glycans in the context of personalized medicine

Viktoria Dotz et al. Biochim Biophys Acta. 2016 Aug.

Abstract

Background: A subset of histo-blood group antigens including ABO and Lewis are oligosaccharide structures which may be conjugated to lipids or proteins. They are known to be important recognition motifs not only in the context of blood transfusions, but also in infection and cancer development.

Scope of review: Current knowledge on the molecular background and the implication of histo-blood group glycans in the prevention and therapy of infectious and non-communicable diseases, such as cancer and cardiovascular disease, is presented.

Major conclusions: Glycan-based histo-blood groups are associated with intestinal microbiota composition, the risk of various diseases as well as therapeutic success of, e.g., vaccination. Their potential as prebiotic or anti-microbial agents, as disease biomarkers and vaccine targets should be further investigated in future studies. For this, recent and future technological advancements will be of particular importance, especially with regard to the unambiguous structural characterization of the glycan portion in combination with information on the protein and lipid carriers of histo-blood group-active glycans in large cohorts.

General significance: Histo-blood group glycans have a unique linking position in the complex network of genes, oncodevelopmental biological processes, and disease mechanisms. Thus, they are highly promising targets for novel approaches in the field of personalized medicine. This article is part of a Special Issue entitled "Glycans in personalised medicine" Guest Editor: Professor Gordan Lauc.

Keywords: Blood group; Cancer; Glycan; Infection; Personalized medicine; Vaccine.

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Figures

Fig. 1
Fig. 1
Examples of human histo-blood group glycans and their carriers on cell surfaces and in body fluids. Histo-blood group glycans decorate various core glycans attached to lipids (black waves) and proteins (blue lines) anchored in the cell membrane, or to secreted glycoproteins/mucins or free oligosaccharides as found in large quantities in human milk. Blood group antigens are found on both N- and O-glycans of proteins. Microbial receptors can recognize various histo-blood group antigens and can thereby attach to the host's epithelial surfaces. Alternatively, soluble glycans can serve as decoy receptors for pathogens.
Fig. 2
Fig. 2
Antigenic structural motifs of the histo-blood groups ABO and Lewis (Le) with their precursors. The interaction of glycosyltransferases acting on type 1 and type 2 precursors results in ABO and Lewis a/b (A) or x/y structures (B), respectively. Mucin-type 3 (T antigen) and glycosphingolipid-based type 4 structures are precursors to ABO and Lewis structures (C). The Ii blood group is determined by linear (i) or beta6-branched (I) polylactosamine type 2 chains (D). Sda antigenic determinant (E). FUT, fucosyltransferase; Se, secretor. Dashed, red-crossed arrows indicate inadmissible reactions.
Fig. 3
Fig. 3
The biosynthetic pathways of the glycosphingolipid-based blood group (BG) antigens. The enzymes and resulting antigens linked to the following BGs are depicted: P1PK BG (A4GALT gene, cyan): Pk, P1, NOR; GLOB BG (B3GALNT1 gene, red): P, PX2; FORS BG (GBGT1, green): FORS1; GLOB collection 209: LKE. For full enzyme names see Table 1. *Each of the structures shown carries a beta-linked ceramide residue at the reducing end glucose, which is not depicted here for simplicity reasons. The links to the synthesis pathways of GSL-based blood group antigens of ABO, Le, and H/Se groups are also shown (gray boxes). Solid lines represent common pathways according to common glycosyltransferase gene alleles, whereas dashed lines symbolize very rare ones. Modified from Refs. , .
Fig. 4
Fig. 4
Oncodevelopmental histo-blood group antigens sialyl-Lea (CA19-9) and sialyl-Lex.
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