Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed beta-Propeller Lectin Family
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F19%3A00107959" target="_blank" >RIV/00216224:14310/19:00107959 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/60461373:22330/19:43920333
Výsledek na webu
<a href="https://www.mdpi.com/1420-3049/24/24/4540" target="_blank" >https://www.mdpi.com/1420-3049/24/24/4540</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/molecules24244540" target="_blank" >10.3390/molecules24244540</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed beta-Propeller Lectin Family
Popis výsledku v původním jazyce
The Photorhabdus species is a Gram-negative bacteria of the family Morganellaceae that is known for its mutualistic relationship with Heterorhabditis nematodes and pathogenicity toward insects. This study is focused on the characterization of the recombinant lectin PLL3 with an origin in P. laumondii subsp. laumondii. PLL3 belongs to the PLL family of lectins with a seven-bladed beta-propeller fold. The binding properties of PLL3 were tested by hemagglutination assay, glycan array, isothermal titration calorimetry, and surface plasmon resonance, and its structure was determined by X-ray crystallography. Obtained data revealed that PLL3 binds similar carbohydrates to those that the other PLL family members bind, with some differences in the binding properties. PLL3 exhibited the highest affinity toward L-fucose and its derivatives but was also able to interact with O-methylated glycans and other ligands.
Název v anglickém jazyce
Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed beta-Propeller Lectin Family
Popis výsledku anglicky
The Photorhabdus species is a Gram-negative bacteria of the family Morganellaceae that is known for its mutualistic relationship with Heterorhabditis nematodes and pathogenicity toward insects. This study is focused on the characterization of the recombinant lectin PLL3 with an origin in P. laumondii subsp. laumondii. PLL3 belongs to the PLL family of lectins with a seven-bladed beta-propeller fold. The binding properties of PLL3 were tested by hemagglutination assay, glycan array, isothermal titration calorimetry, and surface plasmon resonance, and its structure was determined by X-ray crystallography. Obtained data revealed that PLL3 binds similar carbohydrates to those that the other PLL family members bind, with some differences in the binding properties. PLL3 exhibited the highest affinity toward L-fucose and its derivatives but was also able to interact with O-methylated glycans and other ligands.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10600 - Biological sciences
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>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
Údaje specifické pro druh výsledku
Název periodika
Molecules
ISSN
1420-3049
e-ISSN
—
Svazek periodika
24
Číslo periodika v rámci svazku
24
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
20
Strana od-do
1-20
Kód UT WoS článku
000507299600118
EID výsledku v databázi Scopus
2-s2.0-85076495941