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Gram-Negative Flagella Glycosylation
Protein glycosylation had been considered as an eccentricity of a few bacteria. However, through advances in analytical methods and genome sequencing, it is now established that bacteria possess both N-linked and O-linked glycosylation pathways. Both glycosylation pathways can modify multiple protei...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3958885/ https://www.ncbi.nlm.nih.gov/pubmed/24557579 http://dx.doi.org/10.3390/ijms15022840 |
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author | Merino, Susana Tomás, Juan M. |
author_facet | Merino, Susana Tomás, Juan M. |
author_sort | Merino, Susana |
collection | PubMed |
description | Protein glycosylation had been considered as an eccentricity of a few bacteria. However, through advances in analytical methods and genome sequencing, it is now established that bacteria possess both N-linked and O-linked glycosylation pathways. Both glycosylation pathways can modify multiple proteins, flagellins from Archaea and Eubacteria being one of these. Flagella O-glycosylation has been demonstrated in many polar flagellins from Gram-negative bacteria and in only the Gram-positive genera Clostridium and Listeria. Furthermore, O-glycosylation has also been demonstrated in a limited number of lateral flagellins. In this work, we revised the current advances in flagellar glycosylation from Gram-negative bacteria, focusing on the structural diversity of glycans, the O-linked pathway and the biological function of flagella glycosylation. |
format | Online Article Text |
id | pubmed-3958885 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-39588852014-03-20 Gram-Negative Flagella Glycosylation Merino, Susana Tomás, Juan M. Int J Mol Sci Review Protein glycosylation had been considered as an eccentricity of a few bacteria. However, through advances in analytical methods and genome sequencing, it is now established that bacteria possess both N-linked and O-linked glycosylation pathways. Both glycosylation pathways can modify multiple proteins, flagellins from Archaea and Eubacteria being one of these. Flagella O-glycosylation has been demonstrated in many polar flagellins from Gram-negative bacteria and in only the Gram-positive genera Clostridium and Listeria. Furthermore, O-glycosylation has also been demonstrated in a limited number of lateral flagellins. In this work, we revised the current advances in flagellar glycosylation from Gram-negative bacteria, focusing on the structural diversity of glycans, the O-linked pathway and the biological function of flagella glycosylation. Molecular Diversity Preservation International (MDPI) 2014-02-19 /pmc/articles/PMC3958885/ /pubmed/24557579 http://dx.doi.org/10.3390/ijms15022840 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Merino, Susana Tomás, Juan M. Gram-Negative Flagella Glycosylation |
title | Gram-Negative Flagella Glycosylation |
title_full | Gram-Negative Flagella Glycosylation |
title_fullStr | Gram-Negative Flagella Glycosylation |
title_full_unstemmed | Gram-Negative Flagella Glycosylation |
title_short | Gram-Negative Flagella Glycosylation |
title_sort | gram-negative flagella glycosylation |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3958885/ https://www.ncbi.nlm.nih.gov/pubmed/24557579 http://dx.doi.org/10.3390/ijms15022840 |
work_keys_str_mv | AT merinosusana gramnegativeflagellaglycosylation AT tomasjuanm gramnegativeflagellaglycosylation |