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C636 Lectins are sugar-binding proteins or glycoproteins that recognize specific carbohydrate structures and agglutinate various types of animal cells. In marine animals, lectins are believed to contribute as non-self recognition factors to the defense mechanism. Interestingly, it has been theorized that some lectins from marine animals mediate the interaction between symbiont and host. SLL-2 is a D-galactose binding lectin isolated from an octocoral, Sinularia lochmodes. It was found that SLL-2 was distributed densely on the surface of symbiotic dinoflagellate Symbiodinium sp. cells. Previous report showed that SLL-2 transforms free-swimming stage Symbiodinium cells into nonmotile stage Symbiodinium cells and keep them in their non-motile stage [1,2]. These results show that SLL-2 is a chemical cue in the symbiosis between dinoflagellates and coral. The three-dimensional structure of SLL-2 will provide information about the symbiosis mechanism. The structure of SLL-2 was determined by the molecular replacement method using atomic coordinates of Helix pomatia agglutinin (HPA lectin, PDB code: 2ccv) as a search model. Three SLL-2 monomers form a trimer around a non-crystallographic 3-fold axis, and two trimers form a hexameric assembly using hydrogen bonds of three pairs of elongated strands from each monomer. The crystal structure of SLL-2 monomer shows the beta-sandwich lectin fold with six strands. The sites of N-glycosylation and sugar binding (“site 1”) were identified clearly in the monomer structure. In the hexameric molecule, two of the six “site 1”s possess galactopyranoside derivative that might come from the N-glycosylation site, three contain the precipitant molecule, and the remaining one accommodate a water molecule. Crystals from low monosaccharide (GalNAc: N-acetyl-D-Galactosamine) concentration holds three GalNAcs and three precipitant molecules in its “site 1”s. The crystal structure of SLL-2-GalNAc complex from sugar-rich environment indicated that GalNAc molecules bind to all “site 1”s. These observations reveal that SLL-2 can maintain both unsymmetrical and symmetrical hexameric molecule stably across various environments. In addition, a large electron density, which appears for a part of oligosaccharides but was not enough to ensure the bound species and its orientation, was observed at extra sugar binding site, “site 2”. From these results, we could propose binding mode of the pentasaccharide, which is the unbranched polysaccharide recognized by HPA lectin, to SLL-2, and the function of the SLL-2 in the symbiosis between dinoflagellates and coral.

Interface plasmon in pseudo one-dimensional Si/SiO2core-shell nanostructures by electron energy loss spectroscopy

Interface plasmon in pseudo one-dimensional Si/SiO₂core-shell nanostructures by electron energy loss spectroscopy