Seventeen O-acetylated N-glycans and six O-acetylation sites of Myozyme identified using liquid chromatography-tandem mass spectrometry

Park, Heajin; You, Seungkwan; Kim, Jihye; Kim, Woo Seok; Do, Jonghye; Jang, Yeonjoo; Kim, Donghwi; Lee, Junmyoung; Ha, Jongkwan; Oh, Doo-Byoung; Kim, Jae Il; Kim, Ha Hyung

doi:10.1016/j.jpba.2019.03.013

Cited by 12 publications

(13 citation statements)

References 28 publications

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“…Myozyme (Genzyme) is an alpha-glucosidase employed for enzyme replacement therapy for patients with Pompe disease and has at least 6 confirmed N -glycosylation sites. Both mono- and di- O -acetylated sialic acids have been reported on the N -glycans of Myozyme 47 . Aflibercept (Regeneron) is a fusion protein of the extracellular domain of the human VEGF receptor modified and the Fc region of human IgG1 and used for the treatment of metastatic colorectal cancer.…”

Section: Resultsmentioning

confidence: 99%

“…Collectively, the results demonstrate that IM-MS can assign both acetyl ester position and sialic acid linkage type of N -glycans released from biologicals using CCS values of B 1 and B 3 fragment ions. Previously, only compositions of O -acetylated structures could be determined by MS showing the presence of mono- and di- O -acetylated sialosides in Myozyme 47 .…”

Section: Resultsmentioning

confidence: 99%

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Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Vos,

Hooijschuur,

et al. 2023

Nat Commun

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O-acetylation is a common modification of sialic acids that has been implicated in a multitude of biological and disease processes. A lack of analytical methods that can determine exact structures of sialic acid variants is a hurdle to determine roles of distinct O-acetylated sialosides. Here, we describe a drift tube ion mobility-mass spectrometry approach that can elucidate exact O-acetylation patterns as well as glycosidic linkage types of sialosides isolated from complex biological samples. It is based on the use of a library of synthetic O-acetylated sialosides to establish intrinsic collision cross section (CCS) values of diagnostic fragment ions. The CCS values were used to characterize O-acetylated sialosides from mucins and N-linked glycans from biologicals as well as equine tracheal and nasal tissues. It uncovered contrasting sialic acid linkage types of acetylated and non-acetylated sialic acids and provided a rationale for sialic acid binding preferences of equine H7 influenza A viruses.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Vos,

Hooijschuur,

et al. 2023

Nat Commun

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“…Using a similar interpretation method, Park and co-workers demonstrated six O-AcSia sites on recombinant human acid α-glucosidase (Myozyme). 22 The approaches adopted by these two studies, which rely heavily on "expert experience," are difficult to achieve large-scale identification of O-AcSGPs.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Using diagnostic ions for distinguishing different types of sialic acids, Medzihradszky et al identified five O -acetylated O -glycopeptides from Nucleobindin-1 and two O -acetylated N -glycopeptides from Haptoglobin in a mouse. Using a similar interpretation method, Park and co-workers demonstrated six O -AcSia sites on recombinant human acid α-glucosidase (Myozyme) . The approaches adopted by these two studies, which rely heavily on “expert experience,” are difficult to achieve large-scale identification of O -AcSGPs.…”

Section: Introductionmentioning

confidence: 99%

Precision Characterization of Site-Specific O-Acetylated Sialic Acids on N-Glycoproteins

et al. 2023

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O-Acetylation is a common modification of sialic acid, playing a significant role in glycoprotein stability, immune response, and cell development. Due to the lack of efficient methods for direct analysis of O-acetylated sialoglycopeptides (O-AcSGPs), the majority of identified O-acetylated sialic acids (O-AcSia) until now had no glycosite/glycoprotein information. Herein, we introduced a new workflow for precise interpretation of O-AcSGPs with probability estimation by recognizing the characteristic B and Y ions of O-AcSias. With further optimization of mass spectrometry parameters, the method allowed us to identify a total of 171 unique O-AcSGPs in mouse serum. Although the majority of these O-AcSGPs were at a relatively low abundance compared with their non-O-acetylated states, they were mainly involved in peptidase/endopeptidase inhibitor activities. The method paves the way for large-scale structural and functional analyses of site-specific O-AcSias in various complex samples as well as further identification of many other similar chemical modifications on glycoproteins.

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“…The structural characterization of r-hGAA poses a challenge due to the exceptional heterogeneity of the glycan structures (hybrid, complex, and oligomannose type, which may be additionally phosphorylated or acetylated), the different glycan abundances, and the high number of r-hGAA glycosylation sites. Previous studies reported a partial characterization of r-hGAA at the level of released glycans and glycopeptides ( 40 , 41 , 42 , 43 ). In these studies, oligomannose, hybrid-, and complex-type glycan structures were reported also embedding O -acetylation of sialic acids ( 41 ) and phosphorylation of oligomannose structures ( 40 , 41 , 42 , 43 ).…”

mentioning

confidence: 99%

Glycoproteomics of a Single Protein: Revealing Tens of Thousands of Myozyme Glycoforms by Hybrid HPLC-MS Approaches

Marco

Blöchl

Esser‐Skala

et al. 2023

Molecular & Cellular Proteomics

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Seventeen O-acetylated N-glycans and six O-acetylation sites of Myozyme identified using liquid chromatography-tandem mass spectrometry

Cited by 12 publications

References 28 publications

Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Precision Characterization of Site-Specific O-Acetylated Sialic Acids on N-Glycoproteins

Glycoproteomics of a Single Protein: Revealing Tens of Thousands of Myozyme Glycoforms by Hybrid HPLC-MS Approaches

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