Dataset Information

Human Bone Morphogenetic Protein Receptor 2 (BMPR2) N-Glycopeptides

ABSTRACT: Trypsin,Glu-C and trypsin-Glu-C N-glycopeptides spanning all three putative BMPR2 N-glycosylation sites (N29, N84, and N100) were observed. Glycopeptide analyses revealed N-glycan compositions consistent with hybrid and complex glycoforms with abundant fucosylation and sialylation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Valeria Nazaire

LAB HEAD: Kevin Chandler

PROVIDER: PXD066494 | Pride | 2026-07-06

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	2023-12-07-BMPR-2-GluC-Glycoanalysis-0p25ug-1.mzXML	Mzxml
	2023-12-07-BMPR-2-GluC-Glycoanalysis-0p25ug-1.raw	Raw
	2023-12-07-BMPR-2-GluC-Glycoanalysis-0p25ug-2.mzXML	Mzxml
	2023-12-07-BMPR-2-GluC-Glycoanalysis-0p25ug-2.raw	Raw
	2023-12-07-BMPR-2-GluC-Glycoanalysis-0p25ug-3.mzXML	Mzxml

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Publications

Site-Specific Analysis of Bone Morphogenetic Protein Receptor Type 2 N‑Glycosylation Reveals High Heterogeneity at Site Involved in Ligand Binding.

Nazaire Valeria V Garcia Alejandro A Pavan Carlos H CH Chandler Kevin Brown KB

ACS omega 20260619 25

The bone morphogenetic protein receptor type 2 (BMPR2) is expressed in multiple cell types, including endothelial cells, and mediates cell signaling via binding of transforming growth factor β (TGF-β) family ligands, contributing to balanced cell proliferation, apoptosis, and angiogenesis. BMPR2 N-glycosylation reportedly influences ligand binding. Here, we sought to develop a bottom-up nanoliquid chromatography-tandem mass spectrometry method to obtain evidence of site-specific N- ...[more]

PMID: 42395976

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Project description:Recombinant proteins are of great interest in glycobiology and proteomics, known especially for their reproducibility and accessibility. However, variation in glycosylation among recombinant glycoproteins is not well understood and may depend on numerous conditions in the biomanufacturing process. In order to confidently assess variation in glycosylation measurements, it is vital to both optimize the measurement of, and determine the degree of variation between, distributions of glycosylation on specific sites of glycoproteins. This is especially important for glycoproteins that are known to have rapid sequence changes, such as with different influenza strains. In this study, eight strains of recombinant influenza hemagglutinin and neuraminidase produced from HEK293 cell line were obtained from four vendors and digestion was conducted using a series of complex multi-enzymatic methods designed to isolate glycopeptide sequons. Site-specific glycosylation profiles of intact glycopeptides were produced using mass spectrometric evaluation on an orbitrap system and compared using spectral similarity scores. Variation in glycan abundances and distribution was most pronounced between different strains of virus (similarity score = 383 out of 1000), whereas replicates resulted in low variation (similarity score = 957 out of 1000). Glycan variation was also measured based on differences between vendors, lots, batches, protease digestion, and intra-protein site. The most abundant glycans in all of these influenza glycoproteins were monofucosylated and complex, as reported by other laboratories. However, it was found that different vendors can produce very different glycan distributions for the same glycosylation site. Notably, it is demonstrated that glycan distributions are similar for conserved regions of influenza glycoproteins. Overall, these methods present a potential use in developing reproducible measurements of glycosylated biologics for quality control or making more informed decisions in biomanufacturing.

Dataset Information

Human Bone Morphogenetic Protein Receptor 2 (BMPR2) N-Glycopeptides

Dataset's files

Publications

Site-Specific Analysis of Bone Morphogenetic Protein Receptor Type 2 <i>N</i>‑Glycosylation Reveals High Heterogeneity at Site Involved in Ligand Binding.

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Dataset Information

Human Bone Morphogenetic Protein Receptor 2 (BMPR2) N-Glycopeptides

Dataset's files

Publications

Site-Specific Analysis of Bone Morphogenetic Protein Receptor Type 2 &lt;i&gt;N&lt;/i&gt;‑Glycosylation Reveals High Heterogeneity at Site Involved in Ligand Binding.

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OmicsDI is part of the ELIXIR infrastructure

Tweets

Site-Specific Analysis of Bone Morphogenetic Protein Receptor Type 2 <i>N</i>‑Glycosylation Reveals High Heterogeneity at Site Involved in Ligand Binding.