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Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin
BACKGROUND: The 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. Th...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4981971/ https://www.ncbi.nlm.nih.gov/pubmed/27514510 http://dx.doi.org/10.1186/s12866-016-0802-8 |
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author | Wang, Yanchun Wei, Ying Yuan, Shengling Tao, Haoxia Dong, Jie Zhang, Zhaoshan Tian, Wei Liu, Chunjie |
author_facet | Wang, Yanchun Wei, Ying Yuan, Shengling Tao, Haoxia Dong, Jie Zhang, Zhaoshan Tian, Wei Liu, Chunjie |
author_sort | Wang, Yanchun |
collection | PubMed |
description | BACKGROUND: The 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. RESULTS: Biochemical 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. CONCLUSIONS: These data demonstrated that laminin is a ligand for BslA. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12866-016-0802-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4981971 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-49819712016-08-13 Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin Wang, Yanchun Wei, Ying Yuan, Shengling Tao, Haoxia Dong, Jie Zhang, Zhaoshan Tian, Wei Liu, Chunjie BMC Microbiol Research Article BACKGROUND: The 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. RESULTS: Biochemical 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. CONCLUSIONS: These data demonstrated that laminin is a ligand for BslA. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12866-016-0802-8) contains supplementary material, which is available to authorized users. BioMed Central 2016-08-11 /pmc/articles/PMC4981971/ /pubmed/27514510 http://dx.doi.org/10.1186/s12866-016-0802-8 Text en © The Author(s). 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Wang, Yanchun Wei, Ying Yuan, Shengling Tao, Haoxia Dong, Jie Zhang, Zhaoshan Tian, Wei Liu, Chunjie Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin |
title | Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin |
title_full | Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin |
title_fullStr | Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin |
title_full_unstemmed | Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin |
title_short | Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin |
title_sort | bacillus anthracis s-layer protein bsla binds to extracellular matrix by interacting with laminin |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4981971/ https://www.ncbi.nlm.nih.gov/pubmed/27514510 http://dx.doi.org/10.1186/s12866-016-0802-8 |
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