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Surface display of proteins by Gram-negative bacterial autotransporters
Expressing proteins of interest as fusions to proteins of the bacterial envelope is a powerful technique with many biotechnological and medical applications. Autotransporters have recently emerged as a good tool for bacterial surface display. These proteins are composed of an N-terminal signal pepti...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2006
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1533851/ https://www.ncbi.nlm.nih.gov/pubmed/16787545 http://dx.doi.org/10.1186/1475-2859-5-22 |
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author | Rutherford, Nancy Mourez, Michael |
author_facet | Rutherford, Nancy Mourez, Michael |
author_sort | Rutherford, Nancy |
collection | PubMed |
description | Expressing proteins of interest as fusions to proteins of the bacterial envelope is a powerful technique with many biotechnological and medical applications. Autotransporters have recently emerged as a good tool for bacterial surface display. These proteins are composed of an N-terminal signal peptide, followed by a passenger domain and a translocator domain that mediates the outer membrane translocation of the passenger. The natural passenger domain of autotransporters can be replaced by heterologous proteins that become displayed at the bacterial surface by the translocator domain. The simplicity and versatility of this system has made it very attractive and it has been used to display functional enzymes, vaccine antigens as well as polypeptides libraries. The recent advances in the study of the translocation mechanism of autotransporters have raised several controversial issues with implications for their use as display systems. These issues include the requirement for the displayed polypeptides to remain in a translocation-competent state in the periplasm, the requirement for specific signal sequences and "autochaperone" domains, and the influence of the genetic background of the expression host strain. It is therefore important to better understand the mechanism of translocation of autotransporters in order to employ them to their full potential. This review will focus on the recent advances in the study of the translocation mechanism of autotransporters and describe practical considerations regarding their use for bacterial surface display. |
format | Text |
id | pubmed-1533851 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-15338512006-08-08 Surface display of proteins by Gram-negative bacterial autotransporters Rutherford, Nancy Mourez, Michael Microb Cell Fact Review Expressing proteins of interest as fusions to proteins of the bacterial envelope is a powerful technique with many biotechnological and medical applications. Autotransporters have recently emerged as a good tool for bacterial surface display. These proteins are composed of an N-terminal signal peptide, followed by a passenger domain and a translocator domain that mediates the outer membrane translocation of the passenger. The natural passenger domain of autotransporters can be replaced by heterologous proteins that become displayed at the bacterial surface by the translocator domain. The simplicity and versatility of this system has made it very attractive and it has been used to display functional enzymes, vaccine antigens as well as polypeptides libraries. The recent advances in the study of the translocation mechanism of autotransporters have raised several controversial issues with implications for their use as display systems. These issues include the requirement for the displayed polypeptides to remain in a translocation-competent state in the periplasm, the requirement for specific signal sequences and "autochaperone" domains, and the influence of the genetic background of the expression host strain. It is therefore important to better understand the mechanism of translocation of autotransporters in order to employ them to their full potential. This review will focus on the recent advances in the study of the translocation mechanism of autotransporters and describe practical considerations regarding their use for bacterial surface display. BioMed Central 2006-06-20 /pmc/articles/PMC1533851/ /pubmed/16787545 http://dx.doi.org/10.1186/1475-2859-5-22 Text en Copyright © 2006 Rutherford and Mourez; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Rutherford, Nancy Mourez, Michael Surface display of proteins by Gram-negative bacterial autotransporters |
title | Surface display of proteins by Gram-negative bacterial autotransporters |
title_full | Surface display of proteins by Gram-negative bacterial autotransporters |
title_fullStr | Surface display of proteins by Gram-negative bacterial autotransporters |
title_full_unstemmed | Surface display of proteins by Gram-negative bacterial autotransporters |
title_short | Surface display of proteins by Gram-negative bacterial autotransporters |
title_sort | surface display of proteins by gram-negative bacterial autotransporters |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1533851/ https://www.ncbi.nlm.nih.gov/pubmed/16787545 http://dx.doi.org/10.1186/1475-2859-5-22 |
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