Effects of allergic diseases and age on the composition of serum IgG glycome in children

It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients’ IgG glycosylatio...

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Published inScientific reports Vol. 6; no. 1; p. 33198
Main Authors Pezer, Marija, Stambuk, Jerko, Perica, Marija, Razdorov, Genadij, Banic, Ivana, Vuckovic, Frano, Gospic, Adrijana Miletic, Ugrina, Ivo, Vecenaj, Ana, Bakovic, Maja Pucic, Lokas, Sandra Bulat, Zivkovic, Jelena, Plavec, Davor, Devereux, Graham, Turkalj, Mirjana, Lauc, Gordan
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 12.09.2016
Nature Publishing Group
Subjects
631/1647/296
631/250/2152/2153/1291
631/337/458/1524
631/45/221
692/308/3187
82/47
82/58
Affinity chromatography
Age Factors
Allergens
Allergic diseases
Allergies
Carbohydrate Sequence
Case-Control Studies
Child
Child, Preschool
Children
Chromatography
Female
Glycomics
Glycopeptides
Glycosylation
Humanities and Social Sciences
Humans
Hypersensitivity
Hypersensitivity - blood
Hypersensitivity - immunology
Immunoglobulin E
Immunoglobulin G
Immunoglobulin G - blood
Ionization
Ions
Liquid chromatography
Male
Mass spectrometry
Mass spectroscopy
multidisciplinary
Polysaccharides
Protein G
Protein Processing, Post-Translational
Science
Online AccessGet full text
ISSN2045-2322
2045-2322
DOI10.1038/srep33198

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Abstract It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients’ IgG glycosylation profile in allergic diseases. Subclass specific IgG glycosylation profile was analyzed in two cohorts of allergen sensitized and non-sensitized 3- to 11-year-old children (conducted at University of Aberdeen, UK and Children’s Hospital Srebrnjak, Zagreb, Croatia) with 893 subjects in total. IgG was isolated from serum/plasma by affinity chromatography on Protein G. IgG tryptic glycopeptides were analyzed by liquid chromatography electrospray ionization mass spectrometry. In the Zagreb cohort IgG glycome composition changed with age across all IgG subclasses. In both cohorts, IgG glycome composition did not differ in allergen sensitized subjects, nor children sensitized to individual allergens, single allergen mean wheal diameter or positive wheal sum values. In the Zagreb study the results were also replicated for high total serum IgE and in children with self-reported manifest allergic disease. In conclusion, our findings demonstrate no association between serum IgG glycome composition and allergic diseases in children.
AbstractList It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients’ IgG glycosylation profile in allergic diseases. Subclass specific IgG glycosylation profile was analyzed in two cohorts of allergen sensitized and non-sensitized 3- to 11-year-old children (conducted at University of Aberdeen, UK and Children’s Hospital Srebrnjak, Zagreb, Croatia) with 893 subjects in total. IgG was isolated from serum/plasma by affinity chromatography on Protein G. IgG tryptic glycopeptides were analyzed by liquid chromatography electrospray ionization mass spectrometry. In the Zagreb cohort IgG glycome composition changed with age across all IgG subclasses. In both cohorts, IgG glycome composition did not differ in allergen sensitized subjects, nor children sensitized to individual allergens, single allergen mean wheal diameter or positive wheal sum values. In the Zagreb study the results were also replicated for high total serum IgE and in children with self-reported manifest allergic disease. In conclusion, our findings demonstrate no association between serum IgG glycome composition and allergic diseases in children.
It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients' IgG glycosylation profile in allergic diseases. Subclass specific IgG glycosylation profile was analyzed in two cohorts of allergen sensitized and non-sensitized 3- to 11-year-old children (conducted at University of Aberdeen, UK and Children's Hospital Srebrnjak, Zagreb, Croatia) with 893 subjects in total. IgG was isolated from serum/plasma by affinity chromatography on Protein G. IgG tryptic glycopeptides were analyzed by liquid chromatography electrospray ionization mass spectrometry. In the Zagreb cohort IgG glycome composition changed with age across all IgG subclasses. In both cohorts, IgG glycome composition did not differ in allergen sensitized subjects, nor children sensitized to individual allergens, single allergen mean wheal diameter or positive wheal sum values. In the Zagreb study the results were also replicated for high total serum IgE and in children with self-reported manifest allergic disease. In conclusion, our findings demonstrate no association between serum IgG glycome composition and allergic diseases in children.It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients' IgG glycosylation profile in allergic diseases. Subclass specific IgG glycosylation profile was analyzed in two cohorts of allergen sensitized and non-sensitized 3- to 11-year-old children (conducted at University of Aberdeen, UK and Children's Hospital Srebrnjak, Zagreb, Croatia) with 893 subjects in total. IgG was isolated from serum/plasma by affinity chromatography on Protein G. IgG tryptic glycopeptides were analyzed by liquid chromatography electrospray ionization mass spectrometry. In the Zagreb cohort IgG glycome composition changed with age across all IgG subclasses. In both cohorts, IgG glycome composition did not differ in allergen sensitized subjects, nor children sensitized to individual allergens, single allergen mean wheal diameter or positive wheal sum values. In the Zagreb study the results were also replicated for high total serum IgE and in children with self-reported manifest allergic disease. In conclusion, our findings demonstrate no association between serum IgG glycome composition and allergic diseases in children.
ArticleNumber 33198
Author Lokas, Sandra Bulat
Perica, Marija
Plavec, Davor
Turkalj, Mirjana
Bakovic, Maja Pucic
Pezer, Marija
Ugrina, Ivo
Zivkovic, Jelena
Vecenaj, Ana
Stambuk, Jerko
Razdorov, Genadij
Devereux, Graham
Gospic, Adrijana Miletic
Banic, Ivana
Vuckovic, Frano
Lauc, Gordan
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Snippet It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector...
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SubjectTerms 631/1647/296
631/250/2152/2153/1291
631/337/458/1524
631/45/221
692/308/3187
82/47
82/58
Affinity chromatography
Age Factors
Allergens
Allergic diseases
Allergies
Carbohydrate Sequence
Case-Control Studies
Child
Child, Preschool
Children
Chromatography
Female
Glycomics
Glycopeptides
Glycosylation
Humanities and Social Sciences
Humans
Hypersensitivity
Hypersensitivity - blood
Hypersensitivity - immunology
Immunoglobulin E
Immunoglobulin G
Immunoglobulin G - blood
Ionization
Ions
Liquid chromatography
Male
Mass spectrometry
Mass spectroscopy
multidisciplinary
Polysaccharides
Protein G
Protein Processing, Post-Translational
Science
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Title Effects of allergic diseases and age on the composition of serum IgG glycome in children
URI https://link.springer.com/article/10.1038/srep33198
https://www.ncbi.nlm.nih.gov/pubmed/27616597
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https://pubmed.ncbi.nlm.nih.gov/PMC5018987
Volume 6
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