ArticleArchives of microbiology2021
Protein A of Staphylococcus aureus strain NCTC8325 interacted with heparin.
Article in Archives of microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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.
Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Antimicrobial Effect of Gentamicin/Heparin and Gentamicin/Citrate Lock Solutions onInfectious disease reports · 2025Article
- Microbial adaptive pathogenicity strategies to the host inflammatory environment.FEMS microbiology reviews · 2025Review
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Inhibition of bacterial swimming by heparin binding of flagellin FliC from Escherichia coli strain Nissle 1917.Archives of microbiology · 2023Article
- Heparin, Heparan Sulphate and Sepsis: Potential New Options for Treatment.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Staphylococcus aureus binding to Seraph® 100 Microbind® Affinity Filter: Effects of surface protein expression and treatment duration.PloS one · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Heparin, known for its anticoagulant activity, is commonly used as the coatings of medical devices. The attaching of Staphylococcus aureus, a prominent human and animal pathogen, to the heparin coatings usually leads to catheter-related bloodstream infections. Hence, the study of the interaction between heparin and S. aureus surface proteins is desired. Here, we found that protein A (SpA) of S. aureus was a heparin-binding protein, contributing to the interaction between S. aureus and heparin. The cell-wall-anchored SpA was one of the most critical S. aureus virulence factors with a lysin-like motif (LysM). When SpA was mutated to remove the LysM motif, the heparin-binding capability of SpA dropped 50%. The in-frame deletion of spa also reduced the heparin-binding capability of S. aureus. There was 1.3-fold more of heparin bound to wild type S. aureus than the Δspa::Em strain. These results would help understand the host-microbe interaction and the infection by S. aureus.
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What OpenQuestion holds
Registered trials
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.