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The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy
The repeat units of heteropolymeric O antigen are synthesized at the cytosolic side of the inner bacterial membrane via the Wzx/Wzy-dependent assembly pathway. After being translocated across the membrane by Wzx, each repeat unit is polymerized by Wzy to form a glycan chain. In this study, we demons...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498686/ https://www.ncbi.nlm.nih.gov/pubmed/26161781 http://dx.doi.org/10.1371/journal.pone.0131905 |
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author | Merino, Susana Gonzalez, Victor Tomás, Juan M. |
author_facet | Merino, Susana Gonzalez, Victor Tomás, Juan M. |
author_sort | Merino, Susana |
collection | PubMed |
description | The repeat units of heteropolymeric O antigen are synthesized at the cytosolic side of the inner bacterial membrane via the Wzx/Wzy-dependent assembly pathway. After being translocated across the membrane by Wzx, each repeat unit is polymerized by Wzy to form a glycan chain. In this study, we demonstrate the need of the corresponding enzyme transferring the initial HexNAc to undecaprenol phosphate (lipid carrier), together with the corresponding O-antigen polymerase (Wzy), to produce the Aeromonas hydrophila O:34-antigen. We suggest, the concerted action of WecA or P enzyme (UDP-HexNAc: polyprenol-P HexNAc-1-P transferase) and Wzy is involved in the mechanism responsible for the A. hydrophila O-antigen polymerization. |
format | Online Article Text |
id | pubmed-4498686 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-44986862015-07-17 The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy Merino, Susana Gonzalez, Victor Tomás, Juan M. PLoS One Research Article The repeat units of heteropolymeric O antigen are synthesized at the cytosolic side of the inner bacterial membrane via the Wzx/Wzy-dependent assembly pathway. After being translocated across the membrane by Wzx, each repeat unit is polymerized by Wzy to form a glycan chain. In this study, we demonstrate the need of the corresponding enzyme transferring the initial HexNAc to undecaprenol phosphate (lipid carrier), together with the corresponding O-antigen polymerase (Wzy), to produce the Aeromonas hydrophila O:34-antigen. We suggest, the concerted action of WecA or P enzyme (UDP-HexNAc: polyprenol-P HexNAc-1-P transferase) and Wzy is involved in the mechanism responsible for the A. hydrophila O-antigen polymerization. Public Library of Science 2015-07-10 /pmc/articles/PMC4498686/ /pubmed/26161781 http://dx.doi.org/10.1371/journal.pone.0131905 Text en © 2015 Merino et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Merino, Susana Gonzalez, Victor Tomás, Juan M. The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy |
title | The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy |
title_full | The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy |
title_fullStr | The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy |
title_full_unstemmed | The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy |
title_short | The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy |
title_sort | polymerization of aeromonas hydrophila ah-3 o-antigen lps: concerted action of wecp and wzy |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498686/ https://www.ncbi.nlm.nih.gov/pubmed/26161781 http://dx.doi.org/10.1371/journal.pone.0131905 |
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