Production and characterization of galactose-specific lectin PluLec from plant pathogen Photorhabdus luminescens
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F19%3A00112191" target="_blank" >RIV/00216224:14310/19:00112191 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Production and characterization of galactose-specific lectin PluLec from plant pathogen Photorhabdus luminescens
Popis výsledku v původním jazyce
Lectins are a group of proteins of non-immune origin that can reversibly and specifically interact with carbohydrates. They are found in all known living organisms and are involved in recognition events in various physiological and pathological processes like intercellular communication, adhesion, migration and host-pathogen interactions. 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 cell separation and typing. Photorhabdus luminescens is a naturally bioluminescent Gram-negative bacterium which symbiotically lives in Heterorhabditidae nematodes and is strongly pathogenic to insect larvae. PluLec, a putative lectin from Photorhabdus luminescens that we discovered, is 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 structural-functional characterization of recombinant protein PluLec using various methods, namely dynamic light scattering, differential scanning fluorimetry, isothermal titration calorimetry, 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.
Název v anglickém jazyce
Production and characterization of galactose-specific lectin PluLec from plant pathogen Photorhabdus luminescens
Popis výsledku anglicky
Lectins are a group of proteins of non-immune origin that can reversibly and specifically interact with carbohydrates. They are found in all known living organisms and are involved in recognition events in various physiological and pathological processes like intercellular communication, adhesion, migration and host-pathogen interactions. 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 cell separation and typing. Photorhabdus luminescens is a naturally bioluminescent Gram-negative bacterium which symbiotically lives in Heterorhabditidae nematodes and is strongly pathogenic to insect larvae. PluLec, a putative lectin from Photorhabdus luminescens that we discovered, is 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 structural-functional characterization of recombinant protein PluLec using various methods, namely dynamic light scattering, differential scanning fluorimetry, isothermal titration calorimetry, 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.
Klasifikace
Druh
O - Ostatní výsledky
CEP obor
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OECD FORD obor
10600 - Biological sciences
Návaznosti výsledku
Projekt
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Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2019
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů