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Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins
Bacterial surfaces are decorated with carbohydrate structures that may serve as ligands for host receptors. Based on their ability to recognize specific sugar epitopes, plant lectins are extensively used for bacteria typing. We previously observed that the galactose-specific agglutinins from Ricinus...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6215012/ https://www.ncbi.nlm.nih.gov/pubmed/30389954 http://dx.doi.org/10.1038/s41598-018-34383-x |
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author | Kalograiaki, Ioanna Euba, Begoña Fernández-Alonso, María del Carmen Proverbio, Davide St. Geme, Joseph W. Aastrup, Teodor Garmendia, Junkal Cañada, F. Javier Solís, Dolores |
author_facet | Kalograiaki, Ioanna Euba, Begoña Fernández-Alonso, María del Carmen Proverbio, Davide St. Geme, Joseph W. Aastrup, Teodor Garmendia, Junkal Cañada, F. Javier Solís, Dolores |
author_sort | Kalograiaki, Ioanna |
collection | PubMed |
description | Bacterial surfaces are decorated with carbohydrate structures that may serve as ligands for host receptors. Based on their ability to recognize specific sugar epitopes, plant lectins are extensively used for bacteria typing. We previously observed that the galactose-specific agglutinins from Ricinus communis (RCA) and Viscum album (VAA) exhibited differential binding to nontypeable Haemophilus influenzae (NTHi) clinical isolates, their binding being distinctly affected by truncation of the lipooligosaccharide (LOS). Here, we examined their binding to the structurally similar LOS molecules isolated from strains NTHi375 and RdKW20, using microarray binding assays, saturation transfer difference NMR, and molecular dynamics simulations. RCA bound the LOS(RdKW20) glycoform displaying terminal Galβ(1,4)Glcβ, whereas VAA recognized the Galα(1,4)Galβ(1,4)Glcβ epitope in LOS(NTHi375) but not in LOS(RdKW20), unveiling a different presentation. Binding assays to whole bacterial cells were consistent with LOS(NTHi375) serving as ligand for VAA, and also suggested recognition of the glycoprotein HMW1. Regarding RCA, comparable binding to NTHi375 and RdKW20 cells was observed. Interestingly, an increase in LOS(NTHi375) abundance or expression of HMW1 in RdKW20 impaired RCA binding. Overall, the results revealed that, besides the LOS, other carbohydrate structures on the bacterial surface serve as lectin ligands, and highlighted the impact of the specific display of cell surface components on lectin binding. |
format | Online Article Text |
id | pubmed-6215012 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-62150122018-11-06 Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins Kalograiaki, Ioanna Euba, Begoña Fernández-Alonso, María del Carmen Proverbio, Davide St. Geme, Joseph W. Aastrup, Teodor Garmendia, Junkal Cañada, F. Javier Solís, Dolores Sci Rep Article Bacterial surfaces are decorated with carbohydrate structures that may serve as ligands for host receptors. Based on their ability to recognize specific sugar epitopes, plant lectins are extensively used for bacteria typing. We previously observed that the galactose-specific agglutinins from Ricinus communis (RCA) and Viscum album (VAA) exhibited differential binding to nontypeable Haemophilus influenzae (NTHi) clinical isolates, their binding being distinctly affected by truncation of the lipooligosaccharide (LOS). Here, we examined their binding to the structurally similar LOS molecules isolated from strains NTHi375 and RdKW20, using microarray binding assays, saturation transfer difference NMR, and molecular dynamics simulations. RCA bound the LOS(RdKW20) glycoform displaying terminal Galβ(1,4)Glcβ, whereas VAA recognized the Galα(1,4)Galβ(1,4)Glcβ epitope in LOS(NTHi375) but not in LOS(RdKW20), unveiling a different presentation. Binding assays to whole bacterial cells were consistent with LOS(NTHi375) serving as ligand for VAA, and also suggested recognition of the glycoprotein HMW1. Regarding RCA, comparable binding to NTHi375 and RdKW20 cells was observed. Interestingly, an increase in LOS(NTHi375) abundance or expression of HMW1 in RdKW20 impaired RCA binding. Overall, the results revealed that, besides the LOS, other carbohydrate structures on the bacterial surface serve as lectin ligands, and highlighted the impact of the specific display of cell surface components on lectin binding. Nature Publishing Group UK 2018-11-02 /pmc/articles/PMC6215012/ /pubmed/30389954 http://dx.doi.org/10.1038/s41598-018-34383-x Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Kalograiaki, Ioanna Euba, Begoña Fernández-Alonso, María del Carmen Proverbio, Davide St. Geme, Joseph W. Aastrup, Teodor Garmendia, Junkal Cañada, F. Javier Solís, Dolores Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
title | Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
title_full | Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
title_fullStr | Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
title_full_unstemmed | Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
title_short | Differential recognition of Haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
title_sort | differential recognition of haemophilus influenzae whole bacterial cells and isolated lipooligosaccharides by galactose-specific lectins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6215012/ https://www.ncbi.nlm.nih.gov/pubmed/30389954 http://dx.doi.org/10.1038/s41598-018-34383-x |
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