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The Bacterial Biofilm Matrix as a Platform for Protein Delivery
Surface-associated bacterial structures known as biofilms are the target of intense antimicrobial research efforts. We recently identified several secreted proteins that are retained in the bacterial biofilm matrix by their association with the biofilm exopolysaccharide scaffold. Based on our findin...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society of Microbiology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3413402/ https://www.ncbi.nlm.nih.gov/pubmed/22807566 http://dx.doi.org/10.1128/mBio.00127-12 |
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author | Absalon, Cedric Ymele-Leki, Patrick Watnick, Paula I. |
author_facet | Absalon, Cedric Ymele-Leki, Patrick Watnick, Paula I. |
author_sort | Absalon, Cedric |
collection | PubMed |
description | Surface-associated bacterial structures known as biofilms are the target of intense antimicrobial research efforts. We recently identified several secreted proteins that are retained in the bacterial biofilm matrix by their association with the biofilm exopolysaccharide scaffold. Based on our findings, we hypothesized that these problematic bacterial structures might be reengineered to serve as reservoirs for surface-active secreted proteins of biomedical, bioengineering, or biotechnological importance. By piggybacking onto one of these scaffold-associated proteins, we were able to sequester a functional enzyme to the biofilm matrix. We hypothesize that this technology may have diverse applications in vaccine design, digestive disease, and bioremediation. |
format | Online Article Text |
id | pubmed-3413402 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | American Society of Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34134022012-08-07 The Bacterial Biofilm Matrix as a Platform for Protein Delivery Absalon, Cedric Ymele-Leki, Patrick Watnick, Paula I. mBio Opinion/Hypothesis Surface-associated bacterial structures known as biofilms are the target of intense antimicrobial research efforts. We recently identified several secreted proteins that are retained in the bacterial biofilm matrix by their association with the biofilm exopolysaccharide scaffold. Based on our findings, we hypothesized that these problematic bacterial structures might be reengineered to serve as reservoirs for surface-active secreted proteins of biomedical, bioengineering, or biotechnological importance. By piggybacking onto one of these scaffold-associated proteins, we were able to sequester a functional enzyme to the biofilm matrix. We hypothesize that this technology may have diverse applications in vaccine design, digestive disease, and bioremediation. American Society of Microbiology 2012-07-17 /pmc/articles/PMC3413402/ /pubmed/22807566 http://dx.doi.org/10.1128/mBio.00127-12 Text en Copyright © 2012 Absalon et al. http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-nc-sa/3.0/) , which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Opinion/Hypothesis Absalon, Cedric Ymele-Leki, Patrick Watnick, Paula I. The Bacterial Biofilm Matrix as a Platform for Protein Delivery |
title | The Bacterial Biofilm Matrix as a Platform for Protein Delivery |
title_full | The Bacterial Biofilm Matrix as a Platform for Protein Delivery |
title_fullStr | The Bacterial Biofilm Matrix as a Platform for Protein Delivery |
title_full_unstemmed | The Bacterial Biofilm Matrix as a Platform for Protein Delivery |
title_short | The Bacterial Biofilm Matrix as a Platform for Protein Delivery |
title_sort | bacterial biofilm matrix as a platform for protein delivery |
topic | Opinion/Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3413402/ https://www.ncbi.nlm.nih.gov/pubmed/22807566 http://dx.doi.org/10.1128/mBio.00127-12 |
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