Evidence map›Paper›PMID 40542111›Full record

ArticleScientific reports2025

Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.

Max Sommer, Amr Negm, Lasse Outzen, Sabine Windhorst, Azat Gabdulkhakov, Wolfgang Weber, Christian Betzel

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

7 authors.

Max Sommer *Department of Chemistry, Institute of Biochemistry and Molecular Biology, Laboratory for Structural Biology of Infection and Inflammation, University of Hamburg, c/o DESY, Build. 22a. Notkestr. 85, 22603, Hamburg, Germany. m.sommer.92@gmx.de.
Amr Negm *Department of Chemistry, College of Science, King Faisal University, 31982, Al-Ahsa, Saudi Arabia.
Lasse OutzenDepartment of Chemistry, Institute of Pharmacy, University of Hamburg, Bundesstraße 45, 20146, Hamburg, Germany.
Sabine WindhorstInstitute for Biochemistry and Signal transduction, University Medical Center Hamburg-Eppendorf, University Medical Center Hamburg Eppendorf, Martinistraße 52, 20246, Hamburg, Germany.
Azat GabdulkhakovInstitute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.
Wolfgang WeberInstitute of Biochemistry and Molecular Biology I, University Medical Center Hamburg- Eppendorf, Martinistr. 52, 20246, Hamburg, Germany.
Christian BetzelDepartment of Chemistry, Institute of Biochemistry and Molecular Biology, Laboratory for Structural Biology of Infection and Inflammation, University of Hamburg, c/o DESY, Build. 22a. Notkestr. 85, 22603, Hamburg, Germany. christian.betzel@uni-hamburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The increase in infections caused by multi-resistant Gram-negative bacteria, like Stenotrophomonas maltophilia, has become a growing health crisis worldwide. S. maltophilia poses a risk because of its tendency to opportunistically infecting patience for example through colonization of catheters in hospital environments using its intrinsic resistance against multiple antibiotics. Through the COVID-19 pandemic it gained more prominence by being a key pathogen in respiratory co-infections. This study will present a structural analysis of StmPr1, S. maltophilia's main virulence factor, an excreted serine protease. Our study outline structure and functional aspects of StmPr1, revealing a unique autoproteolytic activity resulting in a shortened version of the active enzyme. We also investigated the potential of two groups of peptide-based inhibitors, one being acetyl- and the other being boron-based inhibitors. The focus here lies on Bortezomib, a boron-based serine protease inhibitor, and its potential therapeutic use against S. maltophilia. We provide a structure-function analysis which includes X-ray crystallography data with resolutions ranging from 1.64 to 2.08 Å, molecular dynamic simulations and small-angle X-ray scattering (SAXS) experiments. These data provide a deeper understanding of StmPr1's resilience and mechanisms, while highlighting the relevance of StmPr1's C-terminal extension for correct folding and its stability. Moreover, it also shows that StmPr1 is promising target for further drug discovery investigations to identify compounds and drugs to treat S. maltophilia infections.

Indexed as

Bacterial ProteinsStenotrophomonas maltophiliaVirulence FactorsCOVID-19Crystallography, X-RayGram-Negative Bacterial InfectionsHumansMolecular Dynamics SimulationVirulenceBacterial ProteinsVirulence FactorsBortezomib InhibitionDrug discoveryNosocomial infectionsSerine protease StmPr1Stenotrophomonas maltophiliaStructural biology

Identifiers

PMID40542111
PMCPMC12181431

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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.