J 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
Name: Lektiny a jejich úloha v interakci patogen/hostitel a buněčném rozpoznávání
Investor: Czech Science Foundation
LQ1601, research and development project
Name: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
90127, large research infrastructures
Name: CIISB II