A novel fucose-binding lectin from Photohabdus luminescens (PLL) with an unusual hepta-bladed beta-propeller tetrameric structure


Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity towards insect larvae. A hypothetical protein from P. luminescens was identified, purified from the native source and characterized as an L-fucose-binding lectin, named PLL. Glycan array and biochemical characterization data revealed PLL to be specific towards L-fucose and the disaccharide glycan 3,6-O-Me2-Glcβ1-4(2,3-O-Me2)Rhaα-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homo-tetramer with an inter-subunit disulphide bridge. The crystal structures of native (ntPLL) and recombinant PLL (rPLL) revealed a seven-bladed &beta-propeller fold creating 7 putative fucose-binding sites per monomer. The crystal structure of the rPLL/L-fucose complex confirmed at least three sites being fucose-binding. Moreover, the crystal structures indicated that some of the other sites are masked either by the tetrameric nature of the lectin or by incorporation of the C-terminus of the lectin into one of these sites. PLL exhibited a binding ability to insect haemocytes and the cuticular surface of a nematode, Heterorhabditis bacteriophora.


Atul Kumar1, Petra Sykorva1,2, Gabriel Demo1,3, Pavel Dobles4, Pavel Hyrsl4, and Michaela Wimmerova1,2,3

  • 1. Central European Institute for Technology (CEITEC), Masaryk University, Brno, Czech Republic.
  • 2. Department of Biochemistry, Faculty of Science, Masaryk University, Bron, Czech Republic.
  • 3. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, Czech Republic.
  • 4. Department of Animal Physiology and Immunology, Institute of Experimental Biology, Masaryk University, Brno, Czech Republic


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