Evidence map›Paper›PMID 40626977›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Glycosylation-Dependent Stability of Human Pentraxin-2 Revealed by Surface-Induced Dissociation and Ion Mobility Mass Spectrometry.

Philipp Bittner, Felix Kuhne, Adam Pruška, Julian A Harrison, Natalie Preiss, Markus Haberger, Dietmar Reusch, Renato Zenobi

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Philipp Bittner *Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, Zürich, 8093, Switzerland.ORCID 0000-0001-5094-9538
Felix Kuhne *Analytical Characterization, Pharma Technical Development, Roche Diagnostics GmbH, Nonnenwald 2, 82377, Penzberg, Germany.ORCID 0000-0002-9768-4669
Adam PruškaLaboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, Zürich, 8093, Switzerland.ORCID 0000-0002-5304-2541
Julian A HarrisonLaboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, Zürich, 8093, Switzerland.ORCID 0000-0001-9110-4566
Natalie PreissAnalytical Characterization, Pharma Technical Development, Roche Diagnostics GmbH, Nonnenwald 2, 82377, Penzberg, Germany.
Markus HabergerAnalytical Characterization, Pharma Technical Development, Roche Diagnostics GmbH, Nonnenwald 2, 82377, Penzberg, Germany.
Dietmar ReuschAnalytical Characterization, Pharma Technical Development, Roche Diagnostics GmbH, Nonnenwald 2, 82377, Penzberg, Germany.
Renato ZenobiLaboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, Zürich, 8093, Switzerland.ORCID 0000-0001-5211-4358

Funding

Swiss National Science Foundation 200 020_207 354Swiss National Science Foundation 206021_198122
6 · The paper itself

Abstract

Pentraxin-2 (PTX-2), also known as Serum Amyloid P component, functions as an immunoregulatory glycoprotein and plays a crucial role in fibrotic diseases such as idiopathic pulmonary fibrosis (IPF). Desialylation of PTX-2 has recently been associated with reduced bioactivity and diminished inhibition of fibrocyte differentiation in IPF patients. Each monomer in the naturally assembled pentameric complex is N-glycosylated, predominantly featuring terminal sialic acids on biantennary glycans. However, the influence of these glycoforms on PTX-2's mechanism of action (MoA) and conformational properties has not been comprehensively investigated. In this study, we demonstrate the combined application of surface-induced dissociation (SID) and ion-mobility mass spectrometry (IM-MS) to assess the impact of specific glyco-engineered PTX-2 variants on the stability of its pentameric and decameric complexes. We further explore the effect of individual monomer glycosylation on complex stability. Our results reveal that high levels of terminal sialylation significantly enhance complex stability, whereas desialylation and mannosylation reduce the stability of both pentameric and decameric PTX-2 forms. Regarding the stability of single PTX-2 monomers ejected from the pentamer, in contrast, we found that desialylated and highly mannosylated glycans contribute to the individual monomer stability.

Indexed as

Serum Amyloid P-ComponentGlycosylationHumansIon Mobility SpectrometryMass SpectrometryProtein StabilitySerum Amyloid P-ComponentGlycosylationIon mobility spectrometryNative mass spectrometryPentraxinsSurface‐induced dissociation

Identifiers

PMID40626977
PMCPMC12377442

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.