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 <i>Klebsiella pneumoniae</i> (Kpn) and non-typeable <i>Haemophilus influenzae</i> (NTHi), whic...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-04-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/4/595 |
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| author | María A. Campanero-Rhodes Ioanna Kalograiaki Begoña Euba Enrique Llobet Ana Ardá Jesús Jiménez-Barbero Junkal Garmendia Dolores Solís |
| author_facet | María A. Campanero-Rhodes Ioanna Kalograiaki Begoña Euba Enrique Llobet Ana Ardá Jesús Jiménez-Barbero Junkal Garmendia Dolores Solís |
| author_sort | María A. Campanero-Rhodes |
| collection | DOAJ |
| 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 <i>Klebsiella pneumoniae</i> (Kpn) and non-typeable <i>Haemophilus influenzae</i> (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. |
| first_indexed | 2024-03-10T12:12:20Z |
| format | Article |
| id | doaj.art-34ef3e41066a44f7af834318a3e311fe |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T12:12:20Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-34ef3e41066a44f7af834318a3e311fe2023-11-21T16:06:15ZengMDPI AGBiomolecules2218-273X2021-04-0111459510.3390/biom11040595Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface ArchitecturesMaría A. Campanero-Rhodes0Ioanna Kalograiaki1Begoña Euba2Enrique Llobet3Ana Ardá4Jesús Jiménez-Barbero5Junkal Garmendia6Dolores Solís7Instituto de Química Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, SpainInstituto de Química Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, SpainInstituto de Agrobiotecnología, CSIC-Gobierno Navarra, Avda Pamplona 123, 31192 Mutilva, SpainCIBER de Enfermedades Respiratorias (CIBERES), Avda Monforte de Lemos 3-5, 28029 Madrid, SpainCIC bioGUNE, Basque Research Technology Alliance, BRTA, Bizkaia Technology Park, Building 800, 48160 Derio, SpainCIC bioGUNE, Basque Research Technology Alliance, BRTA, Bizkaia Technology Park, Building 800, 48160 Derio, SpainCIBER de Enfermedades Respiratorias (CIBERES), Avda Monforte de Lemos 3-5, 28029 Madrid, SpainInstituto de Química Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, SpainGalectins 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 <i>Klebsiella pneumoniae</i> (Kpn) and non-typeable <i>Haemophilus influenzae</i> (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.https://www.mdpi.com/2218-273X/11/4/595bacteria microarraysgalectinshost–pathogen interactions<i>Klebsiella pneumoniae</i>non-typeable <i>Haemophilus influenzae</i>lipopolysaccharides |
| spellingShingle | María A. Campanero-Rhodes Ioanna Kalograiaki Begoña Euba Enrique Llobet Ana Ardá Jesús Jiménez-Barbero Junkal Garmendia Dolores Solís Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures Biomolecules bacteria microarrays galectins host–pathogen interactions <i>Klebsiella pneumoniae</i> non-typeable <i>Haemophilus influenzae</i> lipopolysaccharides |
| 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 | bacteria microarrays galectins host–pathogen interactions <i>Klebsiella pneumoniae</i> non-typeable <i>Haemophilus influenzae</i> lipopolysaccharides |
| url | https://www.mdpi.com/2218-273X/11/4/595 |
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