1. Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family
- Author
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Martina Kašáková, N. N. Kondakov, Michaela Wimmerová, Josef Houser, Lukáš Faltinek, Leonid O. Kononov, Filip Melicher, Sébastien Vidal, Kamil Parkan, Eva Fujdiarová, Masaryk University [Brno] (MUNI), University of Chemistry and Technology Prague (UCT Prague), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)
- Subjects
l-fucose ,Glycan ,animal structures ,O-methylated saccharides ,Pharmaceutical Science ,Fructose ,Calorimetry ,Crystallography, X-Ray ,010402 general chemistry ,01 natural sciences ,Protein Structure, Secondary ,Article ,Photorhabdus ,Analytical Chemistry ,law.invention ,03 medical and health sciences ,Bacterial Proteins ,law ,Lectins ,Drug Discovery ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Avidity ,Physical and Theoretical Chemistry ,Surface plasmon resonance ,030304 developmental biology ,0303 health sciences ,Binding Sites ,Hemagglutination assay ,biology ,[CHIM.ORGA]Chemical Sciences/Organic chemistry ,Chemistry ,Organic Chemistry ,Lectin ,Isothermal titration calorimetry ,Surface Plasmon Resonance ,biology.organism_classification ,Recombinant Proteins ,0104 chemical sciences ,Biochemistry ,Chemistry (miscellaneous) ,Recombinant DNA ,biology.protein ,lectin ,Molecular Medicine ,l<%2Fspan>-fucose%22">l-fucose - Abstract
The Photorhabdus species is a Gram-negative bacteria of the family Morganellaceae that is known for its mutualistic relationship with Heterorhabditis nematodes and pathogenicity toward insects. This study is focused on the characterization of the recombinant lectin PLL3 with an origin in P. laumondii subsp. laumondii. PLL3 belongs to the PLL family of lectins with a seven-bladed &beta, propeller fold. The binding properties of PLL3 were tested by hemagglutination assay, glycan array, isothermal titration calorimetry, and surface plasmon resonance, and its structure was determined by X-ray crystallography. Obtained data revealed that PLL3 binds similar carbohydrates to those that the other PLL family members bind, with some differences in the binding properties. PLL3 exhibited the highest affinity toward l-fucose and its derivatives but was also able to interact with O-methylated glycans and other ligands. Unlike the other members of this family, PLL3 was discovered to be a monomer, which might correspond to a weaker avidity effect compared to homologous lectins. Based on the similarity to the related lectins and their proposed biological function, PLL3 might accompany them during the interaction of P. laumondii with both the nematode partner and the insect host.
- Published
- 2019
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