Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family

Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family Full article

Journal

Molecules
ISSN: 1420-3049

Output data

Year: 2019, Volume: 24, Number: 24, Article number : 4540, Pages count : DOI: 10.3390/molecules24244540

Authors

Faltinek Lukáš ¹ , Fujdiarová Eva ^2,3 , Melicher Filip ^2,3 , Houser Josef ^2,3 , Kašáková Martina ⁴ , Kondakov Nikolay ⁵ , Kononov Leonid ⁵ , Parkan Kamil ⁴ , Vidal Sébastien ⁶ , Wimmerová Michaela ^2,3,1

Affiliations

1	Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 611 37 Brno, Czech Republic
2	Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic
3	National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlářská 2, 611 37 Brno, Czech Republic
4	Department of Chemistry of Natural Compounds, University of Chemistry and Technology, Prague (UCTP), Technická 5, 166 28 Prague, Czech Republic
5	N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Prospect 47, Moscow 119 415, Russia
6	Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, CO2-Glyco, UMR 5246, CNRS, Université Claude Bernard Lyon 1, 43 Boulevard du 11 Novembre 1918, 6922 Villeurbanne, France

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 β-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.

Faltinek L. , Fujdiarová E. , Melicher F. , Houser J. , Kašáková M. , Kondakov N. , Kononov L. , Parkan K. , Vidal S. , Wimmerová M.
Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family
Molecules. 2019. V.24. N24. 4540 . DOI: 10.3390/molecules24244540 WOS Scopus OpenAlex

Web of science:	WOS:000507299600118
Scopus:	2-s2.0-85076495941
OpenAlex:	W2996620013

DB	Citing
OpenAlex	5
Scopus	3
Web of science	3