Evidence map›Paper›PMID 39838590›Full record

ArticleMacromolecular bioscience2025

Sulfated Glycosaminoglycans as Inhibitors for Chlamydia Infections: Molecular Weight and Sulfation Dependence.

Sebastian Wintgens, Janita Müller, Felicitas Drees, Dominik Spona, Lorand Bonda, Laura Hartmann, Johannes H Hegemann, Stephan Schmidt

Abstract read
In one paragraph

Article in Macromolecular bioscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

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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.

Sebastian WintgensHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute for Functional Microbial Genomics, 40204, Düsseldorf, Germany.
Janita MüllerHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute for Functional Microbial Genomics, 40204, Düsseldorf, Germany.
Felicitas DreesHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, 40204, Düsseldorf, Germany.
Dominik SponaHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute for Functional Microbial Genomics, 40204, Düsseldorf, Germany.
Lorand BondaHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, 40204, Düsseldorf, Germany.
Laura HartmannHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, 40204, Düsseldorf, Germany.
Johannes H HegemannHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute for Functional Microbial Genomics, 40204, Düsseldorf, Germany.
Stephan SchmidtHeinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, 40204, Düsseldorf, Germany.ORCID 0000-0002-4357-304X

Funding

Deutsche Forschungsgemeinschaft 2748/7-1Deutsche Forschungsgemeinschaft 2748/8-1European Union ERC grant GLYMCE (101088228)
6 · The paper itself

Abstract

Glycosaminoglycans (GAGs) play a pivotal role in pathogen attachment and entry into host cells, where the interaction with GAGs is critical for a diverse range of bacteria and viruses. This study focuses on elucidating the specific interactions between sulfated GAGs and the adhesin OmcB (Outer membrane complex protein B) of Chlamydia species, examining how structural characteristics of GAGs, such as sulfation degree and molecular weight, influence their binding affinity and thereby affect bacterial infectivity. A surface-based binding assay is established to determine the binding constants of OmcB with various GAGs. It is shown that increased sulfation and higher molecular weight enhance GAG binding to OmcB. These findings are further validated using cell assays, which shows that the addition of sulfated GAGs reduces OmcB-cell binding and inhibits the attachment of C. pneumoniae elementary bodies (EBs), underscoring the pivotal role of specific GAGs in chlamydial infections. Notably, heparin exhibites a stronger inhibitory effect on OmcB compare to GAGs with similar sulfation degrees and molecular weights, suggesting that particular molecular architectures may optimize binding interactions.

Indexed as

Bacterial Outer Membrane ProteinsChlamydia InfectionsGlycosaminoglycansSulfatesBacterial AdhesionHumansMolecular WeightProtein BindingBacterial Outer Membrane ProteinsGlycosaminoglycansSulfatescarbohydrate interactioncarrageenanchlamydia pneumoniaechondroitin sulfateGAGsglycansheparan sulfateheparinsulfation

Identifiers

PMID39838590
PMCPMC11995835

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Registered trials

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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.