Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures
| Autor: | Dolores Solís, María Asunción Campanero-Rhodes, Ana Ardá, Jesús Jiménez-Barbero, Begoña Euba, Junkal Garmendia, Ioanna Kalograiaki, Enrique Llobet |
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| Přispěvatelé: | Ministerio de Ciencia, Innovación y Universidades (España), Instituto de Salud Carlos III |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Lipopolysaccharides Glycan Host–pathogen interactions Lipopolysaccharide lipooligosaccharides Galectins Klebsiella pneumoniae Mutant Biochemistry Microbiology Bacterial cell structure Article 03 medical and health sciences chemistry.chemical_compound Bacteria microarrays non-typeable Haemophilus influenzae otorhinolaryngologic diseases Humans Molecular Biology Galectin Binding Sites 030102 biochemistry & molecular biology biology Wild type biology.organism_classification lipopolysaccharides Haemophilus influenzae Lipooligosaccharides QR1-502 stomatognathic diseases 030104 developmental biology chemistry nervous system galectins Docking (molecular) biology.protein bacteria microarrays Nontypeable Haemophilus influenzae Bacteria Protein Binding host–pathogen interactions |
| Zdroj: | Biomolecules Biomolecules, Vol 11, Iss 595, p 595 (2021) Digital.CSIC. Repositorio Institucional del CSIC instname Volume 11 Issue 4 |
| ISSN: | 2218-273X |
| Popis: | 13 pags., 5 figs. -- This article belongs to the Special Issue Galectins: Their Network and Roles in Infection/Immunity/Tumor Growth Control 2021 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. This research was funded by the Spanish Ministry of Science, Innovation, and Universities, the Spanish State Research Agency, and the European Regional Development Fund (Grants RTI2018-099985-B-I00, RTI2018-096369-B-I00, and RTI2018-094751-B-C21, MCIU/AEI/FEDER, UE), and by the CIBER of Respiratory Diseases (CIBERES), an initiative from the Spanish Institute of Health Carlos III (ISCIII). |
| Databáze: | OpenAIRE |
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