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Article

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

1
Instituto de Química Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain
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CIBER de Enfermedades Respiratorias (CIBERES), Avda Monforte de Lemos 3-5, 28029 Madrid, Spain
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Instituto de Agrobiotecnología, CSIC-Gobierno Navarra, Avda Pamplona 123, 31192 Mutilva, Spain
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Optimapharm, ParcBit Edifici Disset A2, 07121 Palma, Spain
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CIC bioGUNE, Basque Research Technology Alliance, BRTA, Bizkaia Technology Park, Building 800, 48160 Derio, Spain
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Ikerbasque, Basque Foundation for Science, 48009 Bilbao, Spain
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Department Organic Chemistry II, Faculty of Science and Technology, UPV-EHU, 48940 Leioa, Spain
*
Author to whom correspondence should be addressed.
Academic Editor: Toshio Hattori
Biomolecules 2021, 11(4), 595; https://doi.org/10.3390/biom11040595
Received: 23 March 2021 / Revised: 13 April 2021 / Accepted: 15 April 2021 / Published: 18 April 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. View Full-Text
Keywords: bacteria microarrays; galectins; host–pathogen interactions; Klebsiella pneumoniae; non-typeable Haemophilus influenzae; lipopolysaccharides; lipooligosaccharides bacteria microarrays; galectins; host–pathogen interactions; Klebsiella pneumoniae; non-typeable Haemophilus influenzae; lipopolysaccharides; lipooligosaccharides
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MDPI and ACS Style

Campanero-Rhodes, M.A.; Kalograiaki, I.; Euba, B.; Llobet, E.; Ardá, A.; Jiménez-Barbero, J.; Garmendia, J.; Solís, D. Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures. Biomolecules 2021, 11, 595. https://doi.org/10.3390/biom11040595

AMA Style

Campanero-Rhodes MA, Kalograiaki I, Euba B, Llobet E, Ardá A, Jiménez-Barbero J, Garmendia J, Solís D. Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures. Biomolecules. 2021; 11(4):595. https://doi.org/10.3390/biom11040595

Chicago/Turabian Style

Campanero-Rhodes, María A., Ioanna Kalograiaki, Begoña Euba, Enrique Llobet, Ana Ardá, Jesús Jiménez-Barbero, Junkal Garmendia, and Dolores Solís. 2021. "Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures" Biomolecules 11, no. 4: 595. https://doi.org/10.3390/biom11040595

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