Evidence map›Paper›PMID 27399672›Full record

ArticleInternational journal of molecular sciences2016

Staphylococcal Superantigen-Like Protein 1 and 5 (SSL1 & SSL5) Limit Neutrophil Chemotaxis and Migration through MMP-Inhibition.

Kirsten J Koymans, Adinda Bisschop, Mignon M Vughs, Kok P M van Kessel, Carla J C de Haas, Jos A G van Strijp

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

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  17. Immune Evasion byMicrobiology spectrum · 2019
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  18. Local Diversification of Methicillin- ResistantFrontiers in microbiology · 2019
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  19. Pathogens (Basel, Switzerland) · 2019
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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

6 authors at 1 institution in 1 country.

Kirsten J KoymansDepartment of Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. k.j.koymans@umcutrecht.nl.
Adinda BisschopDepartment of Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. A.Bisschop@umcutrecht.nl.
Mignon M VughsDepartment of Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. M.M.Vughs@umcutrecht.nl.
Kok P M van KesselDepartment of Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. K.Kessel@umcutrecht.nl.
Carla J C de HaasDepartment of Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. C.J.C.deHaas@umcutrecht.nl.
Jos A G van StrijpDepartment of Medical Microbiology, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands. J.vanStrijp@umcutrecht.nl.
University Medical Center Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are endopeptidases that degrade components of the extracellular matrix, but also modulate inflammation. During bacterial infections, MMPs are important in the recruitment and migration of inflammatory cells. Besides facilitating cell migration by degrading extracellular matrix components, they potentiate the action of several inflammatory molecules, including cytokines, chemokines, and antimicrobial peptides. Staphylococcus aureus secretes an arsenal of immune evasion molecules that interfere with immune cell functioning and hamper proper immune responses. An earlier study identified staphylococcal superantigen-like protein 5 (SSL5) as an MMP9 inhibitor. Since multiple MMPs are involved in neutrophil recruitment, we set up an in-depth search for additional MMP inhibitors by testing a panel of over 70 secreted staphylococcal proteins on the inhibition of the two main neutrophil MMPs: MMP8 (neutrophil collagenase) and MMP9 (neutrophil gelatinase B). We identified SSL1 and SSL5 as potent inhibitors of both neutrophil MMPs and show that they are actually broad range MMP inhibitors. SSL1 and SSL5 prevent MMP-induced cleavage and potentiation of IL-8 and inhibit the migration of neutrophils through collagen. Thus, through MMP-inhibition, SSL1 and SSL5 interfere with neutrophil activation, chemotaxis, and migration, all vital neutrophil functions in bacterial clearance. Studies on MMP-SSL interactions can have therapeutic potential and SSL based derivatives might prove useful in treatment of cancer and destructive inflammatory diseases.

Indexed as

Bacterial ProteinsCell MovementChemotaxisEnzyme-Linked Immunosorbent AssayHumansImmunity, InnateMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesNeutrophilsProtein BindingStaphylococcus aureusU937 CellsBacterial ProteinsMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesSSL5 protein, Staphylococcus aureusenzyme-inhibitorimmune evasioninnate immunitymatrix metalloproteinaseneutrophilS. aureusstaphylococcal superantigen-like proteins

Identifiers

PMID27399672
PMCPMC4964448
OpenAlexW2466711967

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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.