A puzzle piece of protein N-glycosylation in chicken egg: N-glycoproteome of chicken egg vitelline membrane

Xiao, Jing; Wang, Jinqiu; Cheng, Lei; Gao, Sheng; Li, Shugang; Qiu, Ning; Li, Hanmei; Peng, Lianxin; Geng, Fang

doi:10.1016/j.ijbiomac.2020.08.193

Cited by 15 publications

(24 citation statements)

References 43 publications

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“…5 B). Taken together, these results are consistent with our data for chicken egg N-glycoproteomes showing different N-glycosite numbers (15–28) and locations of chicken mucin-5B from differing egg parts ( Xiao et al, 2020 ). This is an “economical and efficient” mode acquired by living organisms in the long-term evolutionary process: a protein template, yielding multiple structures, with various activities.…”

Section: Resultssupporting

confidence: 92%

“…Heterogeneity is one of the important characteristics of glycosylation. Our research group previously demonstrated the tissue specificity of N-glycosylation ( Geng et al, 2017 ; Xiao et al, 2020 ; Yang et al, 2020 ), though other research groups have reported differing N-glycosites of the same protein. Additionally, heterogeneity in the N-glycosylation of milk protein has been documented.…”

Section: Resultsmentioning

confidence: 89%

“…Glycopeptides were enriched via hydrophilic interaction liquid chromatography and deglycosylated with peptide-N-glycosidase F (V4831, Promega Corporation, Madison, WI, USA) in H 2 18 O at 37 °C overnight ( Xiao et al, 2020 ). Deglycopeptides were dissolved in solvent A (aqueous solution containing 0.1% formic acid and 2% acetonitrile) and separated using the LC system (EASY-nLC 1000, Thermo Fisher Scientific, Waltham, USA).…”

Section: Methodsmentioning

confidence: 99%

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Quantitative N-glycoproteome analysis of bovine milk and yogurt

Xiao

Wang

Gan

et al. 2022

Current Research in Food Science

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Post-translational modification structure of food's proteins might be changed during processing, thereby affecting the nutritional characteristics of the food product. In this study, differences in protein N-glycosylation patterns between milk and yogurt were quantitatively compared based on glycopeptide enrichment, liquid chromatography separation, and tandem mass spectrometry analysis. A total of 181 N-glycosites were identified, among which 142 were quantified in milk and yogurt. Significant alterations in the abundance of 13 of these N-glycosites were evident after the fermentation of milk into yogurt. Overall, the N-glycosylation status of the majority of milk proteins remained relatively unchanged in yogurt, suggesting that their conformations, activities, and functions were maintained despite the fermentation process. Among the main milk proteins, N 241 of cathepsin D and N 358 of lactoperoxidase were markedly reduced after undergoing lactic acid fermentation to produce yogurt. Furthermore, a comparative analysis of current and previously reported N-glycoproteomic data revealed heterogeneity in the N-glycosylation of milk proteins. To sum up, a quantitative comparison of the N-glycoproteomes of milk and yogurt was presented here for the first time, providing evidence that the fermentation process of yogurt could cause changes in the N-glycosylation of certain milk proteins.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 89%

Section: Methodsmentioning

confidence: 99%

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Quantitative N-glycoproteome analysis of bovine milk and yogurt

Xiao

Wang

Gan

et al. 2022

Current Research in Food Science

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“…7 Recent research has identified 435 N-glycosylation sites on 208 N-glycoproteins in CEVM, and the N-glycans on apolipoprotein B and vitellogenins were supposed to play directional roles in the compounding of peptide chains and lipids. 8 These results, while preliminary, indicated that N-glycosylation has a pivotal role in CEVM protein functions. Okumura et al reported that ZP1 and ZP3 assembled into helical fibrils through strong interactions between their ZP-C domains to form the inner CEVM, while the N-glycan chains on the ZP1 and ZP3 were exposed on the fibril surface.…”

Section: ■ Introductionmentioning

confidence: 81%

Comparative N-Glycoproteomic Analysis Provides Novel Insights into the Deterioration Mechanisms in Chicken Egg Vitelline Membrane during High-Temperature Storage

Qiu

Mine

et al. 2021

J. Agric. Food Chem.

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The weakening of chicken egg vitelline membrane (CEVM) is one of the most important factors influencing egg quality during high-temperature storage. Therefore, a comparative N-glycoproteomic analysis of CEVM after 10 days of storage at 30 °C was performed to explore the roles of protein N-glycosylation in membrane deterioration. In total, 399 N-glycosites corresponding to 198 proteins were identified, of which 46 N-glycosites from 30 proteins were significantly altered. Gene ontology analysis revealed that these differentially N-glycosylated proteins (DGPs) were involved in antibacterial activity, glycosaminoglycan binding, lipid binding, and aminopeptidase activity. Removal of the N-glycans in Mucin-5B may result in a loss of CEVM’s mechanical properties. The N-glycosites enriched in the apolipoprotein B β2 domain in CEVM were significantly changed, which may contribute to lipid composition modifications during storage. Moreover, N-glycosites in several metalloproteases were located within the functional domain or active site region, indicating that the decreased N-glycosylation levels may affect their structural stability, specific substrate binding, or enzyme activity. These findings provide novel insights into the roles of protein N-glycosylation during membrane weakening.

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“…The supernatant was transferred to hydrophilic interaction liquid chromatography (HILIC) microcolumn and centrifuged at 4,000 × g for 15 min. After three times washing with an enrichment buffer, the glycopeptides were collected from HILIC microcolumn by 10% acetonitrile and dried by vacuum freezing ( Xiao et al, 2020 ). After drying, the glycopeptides were dissolved and digested in 50 μl 50 mM NH 4 CO 3 buffer and 2 μl PNGase F at 37°C overnight.…”

Section: Methodsmentioning

confidence: 99%

Global Profiling of N-Glycoproteins and N-Glycans in the Diatom Phaeodactylum tricornutum

Xie

Chen

et al. 2021

Front. Plant Sci.

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N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteins and N-glycans in microalgae. Here, N-glycoproteomic and N-glycomic approaches were used to unveil the N-glycoproteins and N-glycans in the model diatom Phaeodactylum tricornutum. In total, 863 different N-glycopeptides corresponding to 639 N-glycoproteins were identified from P. tricornutum. These N-glycoproteins participated in a variety of important metabolic pathways in P. tricornutum. Twelve proteins participating in the N-glycosylation pathway were identified as N-glycoproteins, indicating that the N-glycosylation of these proteins might be important for the protein N-glycosylation pathway. Subsequently, 69 N-glycans corresponding to 59 N-glycoproteins were identified and classified into high mannose and hybrid type N-glycans. High mannose type N-glycans contained four different classes, such as Man-5, Man-7, Man-9, and Man-10 with a terminal glucose residue. Hybrid type N-glycan harbored Man-4 with a terminal GlcNAc residue. The identification of N-glycosylation on nascent proteins expanded our understanding of this modification at a N-glycoproteomic scale, the analysis of N-glycan structures updated the N-glycan database in microalgae. The results obtained from this study facilitate the elucidation of the precise function of these N-glycoproteins and are beneficial for future designing the microalga to produce the functional humanized biopharmaceutical N-glycoproteins for the clinical therapeutics.

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A puzzle piece of protein N-glycosylation in chicken egg: N-glycoproteome of chicken egg vitelline membrane

Cited by 15 publications

References 43 publications

Quantitative N-glycoproteome analysis of bovine milk and yogurt

Quantitative N-glycoproteome analysis of bovine milk and yogurt

Comparative N-Glycoproteomic Analysis Provides Novel Insights into the Deterioration Mechanisms in Chicken Egg Vitelline Membrane during High-Temperature Storage

Global Profiling of N-Glycoproteins and N-Glycans in the Diatom Phaeodactylum tricornutum

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