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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...

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Detalles Bibliográficos
Autores principales: Merino, Susana, Tomás, Juan M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2014
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.
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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
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