Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies
| Autoři | |
|---|---|
| Rok publikování | 2014 |
| Druh | Konferenční abstrakty |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | Photorhabdus luminescence is Gram-negative bacilli, exhibit duel nature of lifecycle one, being pathogenic towards insect whereas other, symbiosis with entamo-pathogenic nematodes. The lectin gene was amplified from the genome of P. luminescence and cloned with polyhistidine tag. Expression and production of the lectin was optimized and further purified it using nickel affinity chromatography. The lectin was found to be tetramer of 160 kDa exhibiting 41 kDa monomers interconnected with disulphide bridge. Crystallization of the lectin was achieved after various screening kits and optimized further by hanging drop method. The crystal structure was solved at 1.8 A resolution. The lectin was found to be seven-bladed beta-propeller fold with possibly two different binding sites per monomer. One of the binding site was found to be fucose specific however other was also suggested to be saccharide specificity probably towards a saccharide with higher level of hydroxylation than L-fucopyranose. Lectin was found to exhibit binding ability to haemocytes from insect larvae however was not found to be lethal to Galleria mellonella insect larvae |
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