Glycosylation and Placental Transport of Immunoglobulin G.

Kibe, Tetsuya; Fujimoto, Shinji; Ishida, Chizu; Togari, Hajime; Wada, Yoshiro; Okada, Setsuo; Nakagawa, Hiroaki; Tsukamoto, Yoshinori; Takahashi, Nobutaka

doi:10.3164/jcbn.21.57

Cited by 57 publications

(47 citation statements)

References 13 publications

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“…Two studies in 1995 [34] and 1996 [35] compared the IgG glycosylation of maternal and fetal IgG. The studies analyzed total glycosylation of IgG and described a lower level of agalactosylated structures [34, 35] and higher percentages of galactosylated N-glycan structures [35] for fetal as compared to maternal IgG.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G

et al. 2012

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Human immunoglobulin G (IgG) molecules are composed of two Fab portions and one Fc portion. The glycans attached to the Fc portions of IgG are known to modulate its biological activity as they influence interaction with both complement and various cellular Fc receptors. IgG glycosylation changes significantly with pregnancy, showing a vast increase in galactosylation and sialylation and a concomitant decrease in the incidence of bisecting GlcNAc. Maternal IgGs are actively transported to the fetus by the neonatal Fc receptor (FcRn) expressed in syncytiotrophoblasts in the placenta, providing the fetus and newborn with immunological protection. Two earlier reports described significant differences in total glycosylation between fetal and maternal IgG, suggesting a possible glycosylation-selective transport via the placenta. These results might suggest an alternative maternal transport pathway, since FcRn binding to IgG does not depend on Fc-glycosylation. These early studies were performed by releasing N-glycans from total IgG. Here, we chose for an alternative approach analyzing IgG Fc glycosylation at the glycopeptide level in an Fc-specific manner, providing glycosylation profiles for IgG1 and IgG4 as well as combined Fc glycosylation profiles of IgG2 and 3. The analysis of ten pairs of fetal and maternal IgG samples revealed largely comparable Fc glycosylation for all the analyzed subclasses. Average levels of galactosylation, sialylation, bisecting GlcNAc and fucosylation were very similar for the fetal and maternal IgGs. Our data suggest that the placental IgG transport is not Fc glycosylation selective.

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Section: Introductionmentioning

confidence: 99%

“…The studies analyzed total glycosylation of IgG and described a lower level of agalactosylated structures [34, 35] and higher percentages of galactosylated N-glycan structures [35] for fetal as compared to maternal IgG. These data indicated that there might be a preferential transport of galactosylated IgG to the fetus.…”

Section: Introductionmentioning

confidence: 99%

Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G

et al. 2012

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“…activities [ 1] . In healthy individuals oligosaccharide constituents of IgG are age-related [2,3] and high levels of galactosylation have been observed during pregnancy [4] and among fetuses/newborns [5]. Abnormal glycosylation of IgG was first reported in patients with rheumatoid arthritis (RA), whose IgG exhibited an increase in agalactosyl oligosaccharides lacking outer-arm galactose residues [6].…”

Section: Discussionmentioning

confidence: 99%

Abnormal Glycosylation of IgG as a Clinical Parameter in Patients with Rheumatoid Arthritis: Its Constitutional Analysis by HPLC.

Yuka

Otsuka

Waguri

et al. 1998

J. Clin. Biochem. Nutr.

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SummaryTo determine the abnormal glycosylation patterns of IgG in patients with rheumatoid arthritis (RA), we analyzed these oligosaccharide profiles using a recently established high-performance liquid chromatography (HPLC) method. Oligosaccharides of IgG proteins purified from sera of RA patients were labeled with a fluorescent reagent, 2-aminopyridine. The oligosaccharide derivatives were separated into 12 peaks by HPLC, and compared with those of age-matched controls. Serum IgG from patients with RA (RA-IgG) contained a higher content of oligosaccharides with bisecting GlcNAc than normal IgG, which was accompanied by an increase in the glycosylation of the bisected oligosaccharides. The ratio of the glycosylation of bisected to nonbisected oligosaccharides correlated with RA disease activity as well as with its clinical markers. This ratio reflecting the balance of glycosylation between bisected and nonbisected oligosaccharides may be a useful clinical parameter to monitor RA activity.

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“…67 Interestingly, the FcRn-mediated transport as well as IgG-dependent ADCVI are influenced by the glycosylation pattern of IgG in that only fully glycosylated molecules react with corresponding cellular receptors; alterations and deficiencies of terminal glycan residues result in the diminished receptor reactivity. 68,69 Consequently, the vaginal pH and the glycosylation pattern of IgG may play an important role in the protection or enhanced acquisition of HIV infection. Based on the marked immunological differences in the systemic and mucosal compartments, as well as the unique immunological characteristics of the genital and intestinal tract, with respect to the magnitude, quality, and duration and Ig isotype-dependent effector functions, the mucosal humoral immune responses should be evaluated in parallel with responses in the systemic compartment.…”

Section: Current Controversies and Future Directionsmentioning

confidence: 99%

Humoral Immune Responses to HIV in the Mucosal Secretions and Sera of HIV‐Infected Women

Městecký

Wei

Alexander

et al. 2014

American J Rep Immunol

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Although sera and all external secretions contain antibodies to HIV, their levels, specificity, isotypes, and relevant effector functions display a great degree of variability. Antibodies that bind HIV antigens and neutralize the virus are predominantly associated with the IgG isotype in sera and in all external secretions, even where total levels of IgG are much lower than those of IgA. Rectal fluid that contains high IgA, but low IgG levels, displayed low neutralizing activity independent of antibodies. Therefore, external secretions should be evaluated before and after selective depletion of Ig. At the systemic level, HIV-specific IgA may interfere with the effector functions of IgG, as suggested by recent studies of individuals systemically immunized with an experimental HIV vaccine. Although HIV-specific IgG and IgA antibodies may exhibit their protective activities at mucosal surfaces through interference with viral entry and local neutralization at the systemic level, such antibodies may display discordant effector functions.

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Glycosylation and Placental Transport of Immunoglobulin G.

Cited by 57 publications

References 13 publications

Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G

Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G

Abnormal Glycosylation of IgG as a Clinical Parameter in Patients with Rheumatoid Arthritis: Its Constitutional Analysis by HPLC.

Humoral Immune Responses to HIV in the Mucosal Secretions and Sera of HIV‐Infected Women

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