Detailed Information on Publication Record
2022
Seven-bladed beta-propeller lectins from entomopathogenic bacterium Photorhabdus laumondii
PAULENOVÁ, Eva, Pavel DOBEŠ, Josef HOUSER, Filip MELICHER, Lukáš FALTINEK et. al.Basic information
Original name
Seven-bladed beta-propeller lectins from entomopathogenic bacterium Photorhabdus laumondii
Name in Czech
Lektiny sedmilopatkové betavrtule z hmyzího pathogenu, bakterie Photorhabdus laumondii
Authors
PAULENOVÁ, Eva (203 Czech Republic, belonging to the institution), Pavel DOBEŠ (203 Czech Republic), Josef HOUSER (203 Czech Republic), Filip MELICHER (703 Slovakia), Lukáš FALTINEK (203 Czech Republic), Pavel HYRŠL (203 Czech Republic) and Michaela WIMMEROVÁ (203 Czech Republic)
Edition
XXI setkání biochemniků a molekulárních biologů, 2022
Other information
Language
English
Type of outcome
Prezentace na konferencích
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14310/22:00134027
Organization unit
Faculty of Science
ISBN
978-80-280-0136-0
Keywords (in Czech)
lektin, fenoloxidáza, Photorhabdus, reaktivní formy kyslíku
Keywords in English
lectin; phenoloxidase; Photorhabdus; reactive oxygen species
Změněno: 24/1/2024 15:05, MVDr. Eva Paulenová, Ph.D.
Abstract
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.
Links
GA21-29622S, research and development project |
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