Detailed Information on Publication Record
2021
Heptabladed b-propeller lectins PLL2 and PHL from Photorhabdus spp. recognize O-methylated sugars and influence the host immune system
FUJDIAROVÁ, Eva, Josef HOUSER, Pavel DOBEŠ, Gita PAULÍKOVÁ, Nikolaj KONDAKOV et. al.Basic information
Original name
Heptabladed b-propeller lectins PLL2 and PHL from Photorhabdus spp. recognize O-methylated sugars and influence the host immune system
Authors
FUJDIAROVÁ, Eva (203 Czech Republic, belonging to the institution), Josef HOUSER (203 Czech Republic, belonging to the institution), Pavel DOBEŠ (203 Czech Republic, belonging to the institution), Gita PAULÍKOVÁ (203 Czech Republic, belonging to the institution), Nikolaj KONDAKOV, Leonid KONONOV, Pavel HYRŠL (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)
Edition
The FEBS Journal, Hoboken, Wiley, 2021, 1742-464X
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 5.622
RIV identification code
RIV/00216224:14310/21:00118748
Organization unit
Faculty of Science
UT WoS
000545950100001
Keywords (in Czech)
lektin; O-methylace; fenoloxidáza; Photorhabdus; reaktivní formy kyslíku
Keywords in English
lectin; O-methylation; phenoloxidase; Photorhabdus; reactive oxygen species
Tags
International impact, Reviewed
Změněno: 27/10/2024 15:18, Ing. Martina Blahová
Abstract
V originále
O-methylation is an unusual sugar modification with a function that is not fully understood. Given its occurrence and recognition by lectins involved in the immune response, methylated sugars were proposed to represent a conserved pathogen-associated molecular pattern. We describe the interaction of O-methylated saccharides with two beta-propeller lectins, the newly described PLL2 from the entomopathogenic bacterium Photorhabdus laumondii, and its homologue PHL from the related human pathogen Photorhabdus asymbiotica. The crystal structures of PLL2 and PHL revealed up to 10 out of 14 potential binding sites per protein subunit to be occupied with O-methylated structures. The avidity effect strengthens the interaction by 4 orders of magnitude. PLL2 and PHL also interfere with the early immune response by modulating the production of reactive oxygen species and phenoloxidase activity. Since bacteria from Photorhabdus spp. have a complex life cycle involving pathogenicity towards different hosts, the involvement of PLL2 and PHL might contribute to the pathogen overcoming insect and human immune system defenses in the early stages of infection.
Links
GA18-18964S, research and development project |
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LQ1601, research and development project |
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90127, large research infrastructures |
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