Evidence map›Paper›PMID 26169274›Full record

ArticleInfection and immunity2015

Type II Secretion-Dependent Degradative and Cytotoxic Activities Mediated by Stenotrophomonas maltophilia Serine Proteases StmPr1 and StmPr2.

Ashley L DuMont, Sara M Karaba, Nicholas P Cianciotto

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
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

32 citing papers in PubMed, 40 citations in OpenAlex.

  1. Frontiers in microbiology · 2026
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  10. Frontiers in microbiology · 2024
    Review
  11. Antibiotic Resistance and Virulence Factors in Clinical Isolates ofInternational journal of microbiology · 2024
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  12. A guide toFrontiers in cellular and infection microbiology · 2023
    Review
  13. Clinical challenges treatingJAC-antimicrobial resistance · 2022
    Review
  14. Article
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  18. Review
  19. Genes · 2021
    Review
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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

3 authors at 1 institution in 1 country.

Ashley L DuMontDepartment of Microbiology and Immunology, Northwestern University Medical School, Chicago, Illinois, USA.
Sara M KarabaDepartment of Microbiology and Immunology, Northwestern University Medical School, Chicago, Illinois, USA.
Nicholas P CianciottoDepartment of Microbiology and Immunology, Northwestern University Medical School, Chicago, Illinois, USA n-cianciotto@northwestern.edu.
Northwestern University · US

Funding

TYPE II SECRETION AND LEGIONELLA PNEUMOPHILA INFECTIONR01AI043987 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CIANCIOTTO, NICHOLAS P · 1999 to 2017
$4.8M
Virulence Mechanisms of the Emerging Pathogen Stenotrophomonas maltophiliaR21AI117082 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CIANCIOTTO, NICHOLAS P · 2015 to 2016
$411k
Mechanism of Action of Stenotrophomonas maltophilia proteasesF32AI114130 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DUMONT, ASHLEY LYNN · 2014 to 2016
$177k
NIAID NIH HHS AI043987NIAID NIH HHS AI117082NIAID NIH HHS F32 AI114130NIAID NIH HHS F32AI114130NIAID NIH HHS R01 AI043987NIAID NIH HHS R21 AI117082
6 · The paper itself

Abstract

Stenotrophomonas maltophilia is an emerging opportunistic pathogen that primarily causes pneumonia and bacteremia in immunocompromised individuals. We recently reported that S. maltophilia strain K279a encodes the Xps type II secretion system and that Xps promotes rounding, actin rearrangement, detachment, and death in the human lung epithelial cell line A549. Here, we show that Xps-dependent cell rounding and detachment occur with multiple human and murine cell lines and that serine protease inhibitors block Xps-mediated rounding and detachment of A549 cells. Using genetic analysis, we determined that the serine proteases StmPr1 and StmPr2, which were confirmed to be Xps substrates, are predominantly responsible for secreted proteolytic activities exhibited by strain K279a, as well as the morphological and cytotoxic effects on A549 cells. Supernatants from strain K279a also promoted the degradation of type I collagen, fibrinogen, and fibronectin in a predominantly Xps- and protease-dependent manner, although some Xps-independent degradation of fibrinogen was observed. Finally, Xps, and predominantly StmPr1, degraded interleukin 8 (IL-8) secreted by A549 cells during coculture with strain K279a. Our findings indicate that while StmPr1 and StmPr2 are predominantly responsible for A549 cell rounding, extracellular matrix protein degradation, and IL-8 degradation, additional Xps substrates also contribute to these activities. Altogether, our data provide new insight into the virulence potential of the S. maltophilia Xps type II secretion system and its StmPr1 and StmPr2 substrates.

Indexed as

Bacterial ProteinsCollagen Type IIExtracellular MatrixFibrinogenGram-Negative Bacterial InfectionsHost-Pathogen InteractionsHumansInterleukin-8Protein TransportProteolysisSerine ProteasesStenotrophomonas maltophiliaType II Secretion SystemsBacterial ProteinsCollagen Type IIFibrinogenInterleukin-8Serine ProteasesType II Secretion Systems

Identifiers

PMID26169274
PMCPMC4567643
OpenAlexW2242042268

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.