Comparative analysis of transferrin and IgG N-glycosylation in two human populations

Trbojević‐Akmačić, Irena; Vučković, Frano; Pribić, Tea; Vilaj, Marija; Černigoj, Urh; Vidič, Jana; Šimunović, Jelena; Kepka, Agnieszka; Kolčić, Ivana; Klarić, Lucija; Novokmet, Mislav; Pučić‐Baković, Maja; Rapp, Erdmann; Štrancar, Aleš; Polašek, Ozren; Wilson, James F.; Lauc, Gordan

doi:10.1038/s42003-023-04685-6

Cited by 8 publications

(2 citation statements)

References 68 publications

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“…4a : left) indicated an average acceleration of 3.52 years with a standard deviation of 7.47 years ( P < 0.0001) between predicted age and chronological age in MLWH, compared to their matched MLWoH. As recent studies suggest that the identification of the A2G2S2 glycan trait in isolated IgGs could be a result of transferrin contamination 43 , and despite the high purity of our isolated IgG preparations, as depicted in Supplementary Fig. 1c–e , we evaluated a model excluding the A2G2S2 glycan traits and only including the A2, FA2B, and FA2BG1 glycan traits (Fig.…”

Section: Resultsmentioning

confidence: 77%

Immunoglobulin G N-glycan markers of accelerated biological aging during chronic HIV infection

Giron,

Liu,

Adeniji

et al. 2024

Nat Commun

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People living with HIV (PLWH) experience increased vulnerability to premature aging and inflammation-associated comorbidities, even when HIV replication is suppressed by antiretroviral therapy (ART). However, the factors associated with this vulnerability remain uncertain. In the general population, alterations in the N-glycans on IgGs trigger inflammation and precede the onset of aging-associated diseases. Here, we investigate the IgG N-glycans in cross-sectional and longitudinal samples from 1214 women and men, living with and without HIV. PLWH exhibit an accelerated accumulation of pro-aging-associated glycan alterations and heightened expression of senescence-associated glycan-degrading enzymes compared to controls. These alterations correlate with elevated markers of inflammation and the severity of comorbidities, potentially preceding the development of such comorbidities. Mechanistically, HIV-specific antibodies glycoengineered with these alterations exhibit a reduced ability to elicit anti-HIV Fc-mediated immune activities. These findings hold potential for the development of biomarkers and tools to identify and prevent premature aging and comorbidities in PLWH.

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Section: Resultsmentioning

confidence: 77%

Immunoglobulin G N-glycan markers of accelerated biological aging during chronic HIV infection

Giron,

Liu,

Adeniji

et al. 2024

Nat Commun

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“…12 Cotton filled pipette tips have also been introduced to remove the excess derivatization agent. 13 For highthroughput applications, HILIC plates 14 and carboxyl coated paramagnetic beads 15 have been recommended. While all of these approaches proved useful to remove most of the excess labeling reagent from the reaction mixture, it always entailed an extra sample preparation step with the possibility of losing some of the analyte components.…”

Section: ■ Introductionmentioning

confidence: 99%

Capillary Zone Electrophoresis of 8-Aminopyrene-1,3,6-trisulfonic Acid Labeled Carbohydrates with Online Electrokinetic Sample Cleanup

Farsang,

Hogyor,

Jarvas

et al. 2023

Anal. Chem.

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Capillary electrophoresis is one of the frequently used separation techniques for the analysis of complex carbohydrates. Since sugars lack chromophore or fluorophore groups, their capillary electrophoresis analysis usually requires tagging by a charged fluorophore. To speed up the derivatization reaction, a large excess of the labeling reagent is typically used; therefore, a purification step is necessary prior to CE analysis using the industry standard low-pH gel-buffer system. In addition to representing an extra sample preparation step with the associated labor and cost, the purification process also holds the risk of losing some of the sample components. In this paper we introduce an online electrokinetic sample cleanup process with electroosmotic flow (EOF)-assisted separation in a bare fused silica capillary using alkaline pH background electrolyte and normal polarity separation voltage. 8-Aminopyrene-1,3,6-trisulfonic acid (APTS)-labeled maltooligosaccharides were analyzed first to understand the complex effect of the downstream EOF and the counter current electromigration of the sample components including the labeling dye. The use of 150 mM caproic acid–253 mM Tris (pH 8.1) running buffer facilitated the entrance of the sample components of interest into the separation capillary, while the excess labeling reagent was excluded and, therefore, did not interfere with the detection. The alkaline caproic acid–Tris running buffer was then applied to the N-glycome analysis of human serum samples, showing excellent separation performance, and more importantly, the extra sample purification step was not required.

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Analysis of N‐ and O‐linked site‐specific glycosylation by ion mobility mass spectrometry: State of the art and future directions

Girgis,

Petruncio,

Russo

et al. 2024

Proteomics

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Glycosylation, the major post‐translational modification of proteins, significantly increases the diversity of proteoforms. Glycans are involved in a variety of pivotal structural and functional roles of proteins, and changes in glycosylation are profoundly connected to the progression of numerous diseases. Mass spectrometry (MS) has emerged as the gold standard for glycan and glycopeptide analysis because of its high sensitivity and the wealth of fragmentation information that can be obtained. Various separation techniques have been employed to resolve glycan and glycopeptide isomers at the front end of the MS. However, differentiating structures of isobaric and isomeric glycopeptides constitutes a challenge in MS‐based characterization. Many reports described the use of various ion mobility–mass spectrometry (IM–MS) techniques for glycomic analyses. Nevertheless, very few studies have focused on N‐ and O‐linked site‐specific glycopeptidomic analysis. Unlike glycomics, glycoproteomics presents a multitude of inherent challenges in microheterogeneity, which are further exacerbated by the lack of dedicated bioinformatics tools. In this review, we cover recent advances made towards the growing field of site‐specific glycosylation analysis using IM–MS with a specific emphasis on the MS techniques and capabilities in resolving isomeric peptidoglycan structures. Furthermore, we discuss commonly used software that supports IM–MS data analysis of glycopeptides.

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Comparative analysis of transferrin and IgG N-glycosylation in two human populations

Cited by 8 publications

References 68 publications

Immunoglobulin G N-glycan markers of accelerated biological aging during chronic HIV infection

Immunoglobulin G N-glycan markers of accelerated biological aging during chronic HIV infection

Capillary Zone Electrophoresis of 8-Aminopyrene-1,3,6-trisulfonic Acid Labeled Carbohydrates with Online Electrokinetic Sample Cleanup

Analysis of N‐ and O‐linked site‐specific glycosylation by ion mobility mass spectrometry: State of the art and future directions

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