Research Article

IgG Antibodies to GlcNAcβ and Asialo-GM2 (GA2) Glycans as Potential Markers of Liver Damage in Chronic Hepatitis C and the Efficacy of Antiviral Treatment

Table 2

Brief characterization of glycans and reactivity of human AG IgGs.

Abbreviations, nomenclatureOrigin and reactivity of human IgG Abs

TF, TFα, Galβ1-3GalNAcαCore 1, mucin-type glycan, expressed in tumors. TF is rarely expressed in gut bacteria and was found in Bacteroides ovatus and E. coli. Is present in streptococcal polysaccharides and HCV glycoproteins. In most cases, no or weak reactivity of intravenous IgG Abs to TF was observed [14, 2124].
TFβ, Galβ1-3GalNAcβA constituent of human glycolipids (GM1, Gb5). Present in Bacteroides ovatus and E. coli. Cross-reactivity of Ab to TFαβ, GA1, and Gb5tri was shown [20, 25].
Gb5tri, Galβ1-3GalNAcβ1-3GalThe terminal trisaccharide of Gb5 is expressed in human embryonic and tumor cells and erythrocytes [26, 27].
GA2, GalNAcβ1-4Galβ1-4GlcβReceptor for pathogenic bacteria [28]. Insignificant cross-reactivity to related glycans was observed for serum IgG [29].
Lac-di-NAc, GalNAcβ1-4GlcNAcβGlycans are expressed in tumor cells and parasites [30, 31]. Adhesin for Helicobacter pylori [32].
Tn, GalNAcαMucin-type glycan is related to different diseases and is expressed in tumor cells. Is present in different microorganisms and is a target for mucin-degrading bacteria [21, 33, 34]. Monoreactivity to Tn or partial cross-reactivity to related glycans was shown for anti-Tn IgG [35, 36].
SiaTn, Neu5Acα2-6GalNAcαTumor-associated glycan. An adhesin for viruses and mucin-degrading bacteria [34]. Cross-reactivity to Tn was shown for anti-SiaTn IgG [35, 37].
Adi, GalNAcα1-3GalβA constituent of the A blood group antigen and is a ligand for the spike protein of rotavirus [38]. Is presumably xenogeneic glycan for human. Monoreactivity to Adi or cross-reactivity to related glycans was revealed for anti-Adi IgG [36].
αGal, Bdi, Galα1-3GalβA constituent of the B blood group antigen. Xenogeneic for human and is related to autoimmune disorders. αGal is expressed in pathogenic bacteria (E. coli, Klebsiella, and Salmonella) [39]. Cross-reactivity to related glycans was shown for anti-αGal IgG [36, 40, 41].
FSdi (terminal part of Forssman glycolipid), GalNAcα1-3GalNAcβXenogeneic for human is considered, but recently Fs was revealed in erythrocytes of A(pae) subgroup [42]. Fs-related cross-reactive antigens are present in microbes and animals. Cross-reactivity to related glycans was shown for serum IgG [36].
GlcNAcβA determinant of β-poly-N-acetyl-glucosamine of pathogenic microbes [43]. Is present in human mucin-core structures. Enteric bacteria degrade mucins and produce GlcNAcβ glycans [34, 44]. Partial IgG cross-reactivity to GalNAcβ was revealed [29].
GalNAcβGalNAcβ glycans are synthesized by enteric bacteria [44]. Cross-reactivity to X2di was observed for anti-GalNAcβ IgG [29].
PFdi (outer part of Para-Forssman glycolipid), GalNAcβ1-3GalNAcβPF is a minor component of human erythrocytes [45]. Is a constituent of the cyst wall antigen of Giardia intestinalis [46]. Monoreactivity to PFdi was shown for IgG Abs [29].
X2di (terminal part of X2 glycolipid), GalNAcβ1-3GalβX2 is a minor component of human erythrocytes and other cells. Is associated with the P blood group phenotype [47]. Streptococcal receptor polysaccharides contain similar structures [23]. Monoreactivity to X2di was shown for IgG Abs [29].

In general, the IgG immune profile reflects the high immunogenicity of terminal Gal, GalNAc, and GlcNAc moieties. Besides, IgGs contain specificity to human glycans that are adhesins for viral and bacterial pathogens and/or exotoxins [14].