Novel two-domain lectin from bacterium Photorhabdus laumondii

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F23%3A00133258" target="_blank" >RIV/00216224:14310/23:00133258 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Novel two-domain lectin from bacterium Photorhabdus laumondii

Popis výsledku v původním jazyce

Lectins, saccharide binding proteins, play a key role in the pathogenic processes of diverse bacteria. High interaction specificity enables the recognition of the host cell and adhesion to it. Rather low binding affinity is compensated by a quite strong avidity effect, as lectins are usually polyvalent. Photorhabdus spp., entomopathogenic bacteria, produce various lectins, a few of which have been already characterized. In my work, I focus on producing and characterizing a novel two-domain lectin from Photorhabdus laumondii. First of all, bioinformatical analysis was performed. A synthetic gene was inserted into a production vector and the recombinant protein was produced by E. coli. After production optimization, several methods were used to characterize the binding properties of the recombinant protein, e. g. batch method, and hemagglutination.

Název v anglickém jazyce

Novel two-domain lectin from bacterium Photorhabdus laumondii

Popis výsledku anglicky

Lectins, saccharide binding proteins, play a key role in the pathogenic processes of diverse bacteria. High interaction specificity enables the recognition of the host cell and adhesion to it. Rather low binding affinity is compensated by a quite strong avidity effect, as lectins are usually polyvalent. Photorhabdus spp., entomopathogenic bacteria, produce various lectins, a few of which have been already characterized. In my work, I focus on producing and characterizing a novel two-domain lectin from Photorhabdus laumondii. First of all, bioinformatical analysis was performed. A synthetic gene was inserted into a production vector and the recombinant protein was produced by E. coli. After production optimization, several methods were used to characterize the binding properties of the recombinant protein, e. g. batch method, and hemagglutination.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LM2023042" target="_blank" >LM2023042: Česká infrastruktura pro integrativní strukturní biologii</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů