Evidence map›Paper›PMID 41424281›Full record

ArticleChembiochem : a European journal of chemical biology2026

Staphylococcal SplA and SplB Serine Protease Allelic Variants Exhibit Different Substrate Specificities.

Felix L Glinka, Katharina Mehnert, Lena Koch, Ole Schmöker, Leif Steil, Christian Hentschker, Uwe Völker, Thor B Johannesen, Dominique Böttcher, Michael Lammers and 2 more

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In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2026. 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. Article
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

12 authors.

Felix L GlinkaDept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Katharina MehnertDept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Lena KochDept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Ole SchmökerDept. of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Leif SteilDept. of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17475, Greifswald, Germany.
Christian HentschkerDept. of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17475, Greifswald, Germany.
Uwe VölkerDept. of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, 17475, Greifswald, Germany.
Thor B JohannesenDept. of Sequencing and Bioinformatics, Statens Serum Institut, 2300, Copenhagen, Denmark.
Dominique BöttcherDept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Michael LammersDept. of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Barbara M BrökerInstitute of Immunology, University Medicine Greifswald, 17489, Greifswald, Germany.
Uwe T BornscheuerDept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.ORCID https://orcid.org/0000-0003-0685-2696

Funding

Deutsche Forschungsgemeinschaft Project number 443,535,983Deutsche Forschungsgemeinschaft RTG 2719
6 · The paper itself

Abstract

Staphylococcus aureus is an opportunistic pathogen that is persistently colonizing nearly 30% of the human population and can cause life-threatening infections. S. aureus secretes a variety of virulence factors, such as a set of extracellular serine protease-like proteins (Spls). Spls are expressed by most clinical isolates of S. aureus, but their pathophysiological substrates and role during infection are largely unknown. Pathogens use allelic variation of virulence factors to allow an adaption to different host cells and their defense mechanisms. The differences of these variants are marginally characterized so far. Here, we performed a biochemical characterization of selected allelic variants of the S. aureus SplA and SplB. Our data suggests different variants show differences in their stability, enzymatic activity, and substrate specificity. For the recently identified Spl target proteins RickULP and SseL, different cleavage patterns were observed, upon treatment with different Spl allelic variants. One SplB variant strongly differed in its substrate recognition at the P3/P4 position, more closely resembling SplE than SplB wildtype in its substrate selectivity. Our data provide valuable insights into the evolution of bacterial virulence factors and highlight the importance of including allelic variation of virulence factors to fully understand their role in host-pathogen interaction.

Indexed as

Bacterial ProteinsSerine ProteasesStaphylococcus aureusAllelesHumansSubstrate SpecificityVirulence FactorsBacterial ProteinsSerine ProteasesVirulence Factorsprotein degradationserine protease‐likeSplASplBS taphylococcus aureussubstrate specificity

Identifiers

PMID41424281
PMCPMC12783888

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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.