ArticleBMC microbiology2016
Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin.
Article in BMC microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- The role of human extracellular matrix proteins in defining Staphylococcus aureus biofilm infections.FEMS microbiology reviews · 2024Review
- Binding of the extracellular matrix laminin-1 to Clostridioides difficile strains.Memorias do Instituto Oswaldo Cruz · 2022Article
- Innate Immune Interference Attenuates Inflammation In Bacillus Endophthalmitis.Investigative ophthalmology & visual science · 2020Article
- Increased Excess Intracellular Cyclic di-AMP Levels Impair Growth and Virulence of Bacillus anthracis.Journal of bacteriology · 2020Article
- Slp-coated liposomes for drug delivery and biomedical applications: potential and challenges.International journal of nanomedicine · 2019Review
- Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.The Journal of biological chemistry · 2018Article
- Assembly and Function of the Bacillus anthracis S-Layer.Annual review of microbiology · 2017Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Bacillus anthracis S-layer protein, BslA, plays a crucial role in mammalian infection. BslA is required to mediate adherence between host cells and vegetative forms of bacteria and this interaction promotes target organs adherence and blood-brain barrier (BBB) penetration in vivo. This study attempts to identify the potential eukaryotic ligand(s) for B. anthracis BslA protein.
resultsBiochemical approaches have indicated that the putative host cell ligand(s) for BslA is a surface protein, which is independent of the sugar components for binding to Bs1A. A ligand screening using blot overlays, far Western blots and mass spectrometry analyses revealed that BslA binds to mammalian laminin. ELISA based solid-phase binding assays and surface plasmon resonance assays demonstrated that there were high affinity interactions between BslA(260-652) and laminin. The SPR results also revealed the dissociation constants values of 3.172 × 10(-9)M for the binding of BslA(260-652) to laminin.
conclusionsThese data demonstrated that laminin is a ligand for BslA.
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Identifiers
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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.