Cargando…

Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures

Galectins bind various pathogens through recognition of distinct carbohydrate structures. In this work, we examined the binding of four human galectins to the Gram-negative bacteria Klebsiella pneumoniae (Kpn) and non-typeable Haemophilus influenzae (NTHi), which display different surface glycans. I...

Descripción completa

Detalles Bibliográficos
Autores principales: Campanero-Rhodes, María A., Kalograiaki, Ioanna, Euba, Begoña, Llobet, Enrique, Ardá, Ana, Jiménez-Barbero, Jesús, Garmendia, Junkal, Solís, Dolores
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8074145/
https://www.ncbi.nlm.nih.gov/pubmed/33919637
http://dx.doi.org/10.3390/biom11040595
_version_ 1783684289047560192
author Campanero-Rhodes, María A.
Kalograiaki, Ioanna
Euba, Begoña
Llobet, Enrique
Ardá, Ana
Jiménez-Barbero, Jesús
Garmendia, Junkal
Solís, Dolores
author_facet Campanero-Rhodes, María A.
Kalograiaki, Ioanna
Euba, Begoña
Llobet, Enrique
Ardá, Ana
Jiménez-Barbero, Jesús
Garmendia, Junkal
Solís, Dolores
author_sort Campanero-Rhodes, María A.
collection PubMed
description Galectins bind various pathogens through recognition of distinct carbohydrate structures. In this work, we examined the binding of four human galectins to the Gram-negative bacteria Klebsiella pneumoniae (Kpn) and non-typeable Haemophilus influenzae (NTHi), which display different surface glycans. In particular, Kpn cells are covered by a polysaccharide capsule and display an O-chain-containing lipopolysaccharide (LPS), whereas NTHi is not capsulated and its LPS, termed lipooligosacccharide (LOS), does not contain O-chain. Binding assays to microarray-printed bacteria revealed that galectins-3, -4, and -8, but not galectin-1, bind to Kpn and NTHi cells, and confocal microscopy attested binding to bacterial cells in suspension. The three galectins bound to array-printed Kpn LPS. Moreover, analysis of galectin binding to mutant Kpn cells evidenced that the O-chain is the docking point for galectins on wild type Kpn. Galectins-3, -4, and -8 also bound the NTHi LOS. Microarray-assisted comparison of the binding to full-length and truncated LOSs, as well as to wild type and mutant cells, supported LOS involvement in galectin binding to NTHi. However, deletion of the entire LOS oligosaccharide chain actually increased binding to NTHi cells, indicating the availability of other ligands on the bacterial surface, as similarly inferred for Kpn cells devoid of both O-chain and capsule. Altogether, the results illustrate galectins’ versatility for recognizing different bacterial structures, and point out the occurrence of so far overlooked galectin ligands on bacterial surfaces.
format Online
Article
Text
id pubmed-8074145
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-80741452021-04-27 Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures Campanero-Rhodes, María A. Kalograiaki, Ioanna Euba, Begoña Llobet, Enrique Ardá, Ana Jiménez-Barbero, Jesús Garmendia, Junkal Solís, Dolores Biomolecules Article Galectins bind various pathogens through recognition of distinct carbohydrate structures. In this work, we examined the binding of four human galectins to the Gram-negative bacteria Klebsiella pneumoniae (Kpn) and non-typeable Haemophilus influenzae (NTHi), which display different surface glycans. In particular, Kpn cells are covered by a polysaccharide capsule and display an O-chain-containing lipopolysaccharide (LPS), whereas NTHi is not capsulated and its LPS, termed lipooligosacccharide (LOS), does not contain O-chain. Binding assays to microarray-printed bacteria revealed that galectins-3, -4, and -8, but not galectin-1, bind to Kpn and NTHi cells, and confocal microscopy attested binding to bacterial cells in suspension. The three galectins bound to array-printed Kpn LPS. Moreover, analysis of galectin binding to mutant Kpn cells evidenced that the O-chain is the docking point for galectins on wild type Kpn. Galectins-3, -4, and -8 also bound the NTHi LOS. Microarray-assisted comparison of the binding to full-length and truncated LOSs, as well as to wild type and mutant cells, supported LOS involvement in galectin binding to NTHi. However, deletion of the entire LOS oligosaccharide chain actually increased binding to NTHi cells, indicating the availability of other ligands on the bacterial surface, as similarly inferred for Kpn cells devoid of both O-chain and capsule. Altogether, the results illustrate galectins’ versatility for recognizing different bacterial structures, and point out the occurrence of so far overlooked galectin ligands on bacterial surfaces. MDPI 2021-04-18 /pmc/articles/PMC8074145/ /pubmed/33919637 http://dx.doi.org/10.3390/biom11040595 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Campanero-Rhodes, María A.
Kalograiaki, Ioanna
Euba, Begoña
Llobet, Enrique
Ardá, Ana
Jiménez-Barbero, Jesús
Garmendia, Junkal
Solís, Dolores
Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
title Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
title_full Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
title_fullStr Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
title_full_unstemmed Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
title_short Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
title_sort exploration of galectin ligands displayed on gram-negative respiratory bacterial pathogens with different cell surface architectures
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8074145/
https://www.ncbi.nlm.nih.gov/pubmed/33919637
http://dx.doi.org/10.3390/biom11040595
work_keys_str_mv AT campanerorhodesmariaa explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT kalograiakiioanna explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT eubabegona explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT llobetenrique explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT ardaana explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT jimenezbarberojesus explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT garmendiajunkal explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures
AT solisdolores explorationofgalectinligandsdisplayedongramnegativerespiratorybacterialpathogenswithdifferentcellsurfacearchitectures