2022
Seven-bladed beta-propeller lectins from entomopathogenic bacterium Photorhabdus laumondii
PAULENOVÁ, Eva, Pavel DOBEŠ, Josef HOUSER, Filip MELICHER, Lukáš FALTINEK et. al.Základní údaje
Originální název
Seven-bladed beta-propeller lectins from entomopathogenic bacterium Photorhabdus laumondii
Název česky
Lektiny sedmilopatkové betavrtule z hmyzího pathogenu, bakterie Photorhabdus laumondii
Autoři
PAULENOVÁ, Eva (203 Česká republika, domácí), Pavel DOBEŠ (203 Česká republika), Josef HOUSER (203 Česká republika), Filip MELICHER (703 Slovensko), Lukáš FALTINEK (203 Česká republika), Pavel HYRŠL (203 Česká republika) a Michaela WIMMEROVÁ (203 Česká republika)
Vydání
XXI setkání biochemniků a molekulárních biologů, 2022
Další údaje
Jazyk
angličtina
Typ výsledku
Prezentace na konferencích
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/22:00134027
Organizační jednotka
Přírodovědecká fakulta
ISBN
978-80-280-0136-0
Klíčová slova česky
lektin, fenoloxidáza, Photorhabdus, reaktivní formy kyslíku
Klíčová slova anglicky
lectin; phenoloxidase; Photorhabdus; reactive oxygen species
Změněno: 24. 1. 2024 15:05, MVDr. Eva Paulenová, Ph.D.
Anotace
V originále
Bacteria from the genus Photorhabdus are known for a complicated life cycle that involves symbiosis with nematodes of the genus Heterorhabditis and pathogenicity towards insects The complicated life cycle of Photorhabdus-Heterorhabditis complex is thoroughly studied and very well described. Photorhabdus has three distinct and obligatory roles to play in the life cycle. First, kill the insect host; second, support the nematode development and growth; third, colonize the gut of newly formed IJs. In all these roles, lectins could be involved. Lectins, in general, are a well-known group of proteins capable of binding saccharide compounds with unusually high specificity. They facilitate cell-to-cell interactions on the molecular level in multiple physiological and pathophysiological processes throughout nature. In this work, we focus on the characterization of 5 structurally related lectins from P. laumondii subsp. laumondii TT01. Various methods were used to determine their binding specificity and structure (e.g. glycan array, isothermal titration calorimetry, X-ray crystallography). To determine their biological function, experiments with insect hemocytes and nematode symbiont were conducted. The production of lectins during bacterial growth was monitored with qPCR. The results suggest that these lectins are involved in the early stages of the infection, helping Photorhabdus to overcome the host defense mechanisms.
Návaznosti
GA21-29622S, projekt VaV |
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