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Production and characterization of two-domain lectins from Photorhabdus spp.

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F23%3A00133678" target="_blank" >RIV/00216224:14310/23:00133678 - isvavai.cz</a>

  • Výsledek na webu

  • DOI - Digital Object Identifier

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Production and characterization of two-domain lectins from Photorhabdus spp.

  • Popis výsledku v původním jazyce

    Lectins are proteins that non-covalently and reversibly bind saccharides. They are ubiquitous, found in organisms of all kingdoms, and interact, for example, with carbohydrate groups found on the surface of cells. Bacteria use the properties of lectins to recognize host cells and attach to them. Bacterial infection cannot occur without prior adhesion, and this is where lectins play an important role. Genes encoding lectins have been found in the genomes of various bacteria, including Photorhabdus spp. Photorhabdus spp. are Gram-negative bacteria that combine mutualistic and pathogenic processes during their life cycle. They live in a mutualistic relationship with nematodes Heterorhabditis spp. with which they form a pathogenic complex. Together they infect mostly insects, though some species are also human opportunistic pathogens. In this research, we focus on the characterization of a group of two-domain lectins from P. laumondii. Basic bioinformatic analysis was used to predict the properties of these proteins. One of the proteins, named PpxD, was selected for further characterization. Cloning and production of the recombinant protein was performed. The binding properties of the PpxD protein were characterized by the batch method and hemagglutination assay.

  • Název v anglickém jazyce

    Production and characterization of two-domain lectins from Photorhabdus spp.

  • Popis výsledku anglicky

    Lectins are proteins that non-covalently and reversibly bind saccharides. They are ubiquitous, found in organisms of all kingdoms, and interact, for example, with carbohydrate groups found on the surface of cells. Bacteria use the properties of lectins to recognize host cells and attach to them. Bacterial infection cannot occur without prior adhesion, and this is where lectins play an important role. Genes encoding lectins have been found in the genomes of various bacteria, including Photorhabdus spp. Photorhabdus spp. are Gram-negative bacteria that combine mutualistic and pathogenic processes during their life cycle. They live in a mutualistic relationship with nematodes Heterorhabditis spp. with which they form a pathogenic complex. Together they infect mostly insects, though some species are also human opportunistic pathogens. In this research, we focus on the characterization of a group of two-domain lectins from P. laumondii. Basic bioinformatic analysis was used to predict the properties of these proteins. One of the proteins, named PpxD, was selected for further characterization. Cloning and production of the recombinant protein was performed. The binding properties of the PpxD protein were characterized by the batch method and hemagglutination assay.

Klasifikace

  • Druh

    O - Ostatní výsledky

  • CEP obor

  • OECD FORD obor

    10608 - Biochemistry and molecular biology

Návaznosti výsledku

  • 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

Ostatní

  • Rok uplatnění

    2023

  • Kód důvěrnosti údajů

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