Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein.
The self-associating autotransporters (SAATs) are multifunctional secreted proteins of Escherichia coli, comprising the AIDA-I, TibA and Ag43 proteins. One of their characteristics is that they can be glycosylated. Glycosylation of AIDA-I and Ag43 have been investigated, but not that of TibA. It is...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3835316?pdf=render |
| _version_ | 1828158470411517952 |
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| author | Jean-Philippe Côté Marie-Ève Charbonneau Michael Mourez |
| author_facet | Jean-Philippe Côté Marie-Ève Charbonneau Michael Mourez |
| author_sort | Jean-Philippe Côté |
| collection | DOAJ |
| description | The self-associating autotransporters (SAATs) are multifunctional secreted proteins of Escherichia coli, comprising the AIDA-I, TibA and Ag43 proteins. One of their characteristics is that they can be glycosylated. Glycosylation of AIDA-I and Ag43 have been investigated, but not that of TibA. It is still not clear whether glycosylation of the SAATs affect their structure or their functionality. Therefore, we have looked at the effects of glycosylation on the TibA adhesin/invasin. TibA is glycosylated by TibC, a specific glycosyltransferase, and the two genes are encoded in an operon. In this study, we have found that the glycosylation of TibA is not limited to the extracellular functional domain, as previously observed with AIDA-I and Ag43. We have determined that unglycosylated TibA is not able to promote the adhesion of bacteria on cultured epithelial cell, even though it is still able to promote invasion, biofilm formation and autoaggregation of bacteria. We have purified the glycosylated and unglycosylated forms of TibA, and determined that TibA is less stable when not glycosylated. We finally observed that glycosylation affects the oligomerisation of TibA and that unglycosylated TibA is locked in a conformation that is not suited for adhesion. Our results suggest that the effect of glycosylation on the functionality of TibA is indirect. |
| first_indexed | 2024-04-11T23:45:50Z |
| format | Article |
| id | doaj.art-c6e341424be64781af67a3abc4001b6d |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-11T23:45:50Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-c6e341424be64781af67a3abc4001b6d2022-12-22T03:56:39ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-01811e8073910.1371/journal.pone.0080739Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein.Jean-Philippe CôtéMarie-Ève CharbonneauMichael MourezThe self-associating autotransporters (SAATs) are multifunctional secreted proteins of Escherichia coli, comprising the AIDA-I, TibA and Ag43 proteins. One of their characteristics is that they can be glycosylated. Glycosylation of AIDA-I and Ag43 have been investigated, but not that of TibA. It is still not clear whether glycosylation of the SAATs affect their structure or their functionality. Therefore, we have looked at the effects of glycosylation on the TibA adhesin/invasin. TibA is glycosylated by TibC, a specific glycosyltransferase, and the two genes are encoded in an operon. In this study, we have found that the glycosylation of TibA is not limited to the extracellular functional domain, as previously observed with AIDA-I and Ag43. We have determined that unglycosylated TibA is not able to promote the adhesion of bacteria on cultured epithelial cell, even though it is still able to promote invasion, biofilm formation and autoaggregation of bacteria. We have purified the glycosylated and unglycosylated forms of TibA, and determined that TibA is less stable when not glycosylated. We finally observed that glycosylation affects the oligomerisation of TibA and that unglycosylated TibA is locked in a conformation that is not suited for adhesion. Our results suggest that the effect of glycosylation on the functionality of TibA is indirect.http://europepmc.org/articles/PMC3835316?pdf=render |
| spellingShingle | Jean-Philippe Côté Marie-Ève Charbonneau Michael Mourez Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein. PLoS ONE |
| title | Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein. |
| title_full | Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein. |
| title_fullStr | Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein. |
| title_full_unstemmed | Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein. |
| title_short | Glycosylation of the Escherichia coli TibA self-associating autotransporter influences the conformation and the functionality of the protein. |
| title_sort | glycosylation of the escherichia coli tiba self associating autotransporter influences the conformation and the functionality of the protein |
| url | http://europepmc.org/articles/PMC3835316?pdf=render |
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