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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%2F60461373%3A22330%2F19%3A43920333" target="_blank" >RIV/60461373:22330/19:43920333 - isvavai.cz</a>

  • Nalezeny alternativní kódy

    RIV/00216224:14310/19:00107959

  • Výsledek na webu

    <a href="https://www.mdpi.com/1420-3049/24/24/4540/htm" target="_blank" >https://www.mdpi.com/1420-3049/24/24/4540/htm</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. Unlike the other members of this family, PLL3 was discovered to be a monomer, which might correspond to a weaker avidity effect compared to homologous lectins. Based on the similarity to the related lectins and their proposed biological function, PLL3 might accompany them during the interaction of P. laumondii with both the nematode partner and the insect host.

  • 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. Unlike the other members of this family, PLL3 was discovered to be a monomer, which might correspond to a weaker avidity effect compared to homologous lectins. Based on the similarity to the related lectins and their proposed biological function, PLL3 might accompany them during the interaction of P. laumondii with both the nematode partner and the insect host.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10608 - Biochemistry and molecular biology

Návaznosti výsledku

  • Projekt

  • Návaznosti

    S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

  • Kód UT WoS článku

    000507299600118

  • EID výsledku v databázi Scopus

    2-s2.0-85076495941