Characterization of PluLec, a novel galactose-specific lectin from Photorhabdus luminescens
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| Year of publication | 2018 |
| Type | Conference abstract |
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| Description | Lectins are proteins of non-immune origin capable of binding carbohydrates reversibly and with high specificity. They are found in all known living organisms. Unlike antibodies, they are not product of immune response and do not possess any enzymatic activity. Lectins are involved in recognition events in various physiological and pathological processes (e.g. cell communication, adhesion, migration, pathogen recognition, immune response modulation). Lectins are commonly used for characterization of carbohydrate structures, for purification of glycoproteins and to specifically label the cell surface structures. They are also used for separation and cell typing. Photorhabdus luminescens is a naturally bioluminescent Gram-negative bacterium and an insect pathogen, which symbiotically lives in Heterorhabditidae nematodes. PluLec is a putative lectin from Photorhabdus luminescens and a homologue of PA-IL lectin, which is D-galactose specific, Ca2+ dependent, cytotoxic lectin from opportunistic pathogen Pseudomonas aeruginosa, involved in facilitating infection in patients with compromised immunity. This research is focused on cloning, production and study of recombinant protein PluLec using various methods for structural and functional characterization, namely dynamic light scattering, circular dichroism, differential scanning fluorimetry, hemagglutination, glycan array, surface plasmon resonance, analytical ultracentrifugation and protein X-ray crystallography. Detailed knowledge of the structure and function of PluLec can help to understand the mechanism of P. luminescens infection. The lectin might also find further application in biotechnological research. |
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