Detailed Information on Publication Record

FUJDIAROVÁ, Eva, Pavel DOBEŠ and Michaela WIMMEROVÁ. Study of lectins from Photorhabdus luminescens bacterium. In The 43rd FEBS congress Prague. 2018.

Other formats: BibTeX LaTeX RIS

TY  - CONF
ID  - 1431758
AU  - Fujdiarová, Eva - Dobeš, Pavel - Wimmerová, Michaela
PY  - 2018
TI  - Study of lectins from Photorhabdus luminescens bacterium
KW  - lectins
KW  - Photorhabdus luminescens
KW  - Heterorhabditis bacteriophora
KW  - glycan-array
KW  - ROS
KW  - crystallography
UR  - https://2018.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170093099099099100424170
L2  - https://2018.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170093099099099100424170
N2  - We present novel lectins from Photorhabdus luminescens with an unusual heptabladed beta-propeller fold. These proteins show very high sequence identity with recently described lectins PLL and PHL from the Photorhabdus genus. Furthermore, all lectins are localized in a row in a bacterial genome. Lectins, a group of proteins capable of binding glycoconjugates specifically and reversibly, are showing their importance in both mutualistic and parasitic interactions between microorganism and hosts. Both of these stages are present in the P. luminescens life cycle. The bacterium is highly pathogenic towards the larval stadium of various insect species and mutualistic with infective juveniles of the nematode Heterorhabditis bacteriophora. For structural and functional characterization of Photorhabdus lectins, the wide range of methods was used, e.g. glycan array, surface plasmon resonance, isothermal titration calorimetry, analytical ultracentrifugation, X-ray crystallography and biological assays performed with human blood and hemolymph (reactive oxygen species production and phenoloxidase activity). Whereas heptabladed beta-propeller fold is common for all studied lectins, the oligomeric state differs from mono- to di-mer. All studied lectins recognize L-fucose and O-methylated disaccharide glucose(1-4)rhamnose, but the fine binding specificities vary. The biological assay shows inhibition of the immune system response in the presence of P. luminescens lectins. Our results indicate these lectins might be involved in P. luminescens pathogenicity towards insect larva.
ER  -

Basic information
Original name	Study of lectins from Photorhabdus luminescens bacterium
Name in Czech	Studie lektinů z bakterie Photorhabdus luminescens
Authors	FUJDIAROVÁ, Eva (203 Czech Republic, belonging to the institution), Pavel DOBEŠ (203 Czech Republic) and Michaela WIMMEROVÁ (203 Czech Republic).
Edition	The 43rd FEBS congress Prague, 2018.

Other information
Original language	English
Type of outcome	Conference abstract
Field of Study	10700 1.7 Other natural sciences
Country of publisher	Czech Republic
Confidentiality degree	is not subject to a state or trade secret
WWW	URL
RIV identification code	RIV/00216224:14310/18:00103557
Organization unit	Faculty of Science
Keywords (in Czech)	lektiny; Photorhabdus luminescens; Heterorhabditis bacteriophora; glycan-array; ROS; krystalografie
Keywords in English	lectins; Photorhabdus luminescens; Heterorhabditis bacteriophora; glycan-array; ROS; crystallography
Changed by	Changed by: MVDr. Eva Paulenová, Ph.D., učo 437375. Changed: 3/9/2018 14:04.

Abstract
We present novel lectins from Photorhabdus luminescens with an unusual heptabladed beta-propeller fold. These proteins show very high sequence identity with recently described lectins PLL and PHL from the Photorhabdus genus. Furthermore, all lectins are localized in a row in a bacterial genome. Lectins, a group of proteins capable of binding glycoconjugates specifically and reversibly, are showing their importance in both mutualistic and parasitic interactions between microorganism and hosts. Both of these stages are present in the P. luminescens life cycle. The bacterium is highly pathogenic towards the larval stadium of various insect species and mutualistic with infective juveniles of the nematode Heterorhabditis bacteriophora. For structural and functional characterization of Photorhabdus lectins, the wide range of methods was used, e.g. glycan array, surface plasmon resonance, isothermal titration calorimetry, analytical ultracentrifugation, X-ray crystallography and biological assays performed with human blood and hemolymph (reactive oxygen species production and phenoloxidase activity). Whereas heptabladed beta-propeller fold is common for all studied lectins, the oligomeric state differs from mono- to di-mer. All studied lectins recognize L-fucose and O-methylated disaccharide glucose(1-4)rhamnose, but the fine binding specificities vary. The biological assay shows inhibition of the immune system response in the presence of P. luminescens lectins. Our results indicate these lectins might be involved in P. luminescens pathogenicity towards insect larva.

Abstract

We present novel lectins from Photorhabdus luminescens with an unusual heptabladed beta-propeller fold. These proteins show very high sequence identity with recently described lectins PLL and PHL from the Photorhabdus genus. Furthermore, all lectins are localized in a row in a bacterial genome. Lectins, a group of proteins capable of binding glycoconjugates specifically and reversibly, are showing their importance in both mutualistic and parasitic interactions between microorganism and hosts. Both of these stages are present in the P. luminescens life cycle. The bacterium is highly pathogenic towards the larval stadium of various insect species and mutualistic with infective juveniles of the nematode Heterorhabditis bacteriophora. For structural and functional characterization of Photorhabdus lectins, the wide range of methods was used, e.g. glycan array, surface plasmon resonance, isothermal titration calorimetry, analytical ultracentrifugation, X-ray crystallography and biological assays performed with human blood and hemolymph (reactive oxygen species production and phenoloxidase activity). Whereas heptabladed beta-propeller fold is common for all studied lectins, the oligomeric state differs from mono- to di-mer. All studied lectins recognize L-fucose and O-methylated disaccharide glucose(1-4)rhamnose, but the fine binding specificities vary. The biological assay shows inhibition of the immune system response in the presence of P. luminescens lectins. Our results indicate these lectins might be involved in P. luminescens pathogenicity towards insect larva.

Links
GA18-18964S, interní kód MU	Name: Lektiny a jejich úloha v interakci patogen/hostitel a buněčném rozpoznávání
GA18-18964S, interní kód MU	Investor: Czech Science Foundation
LQ1601, research and development project	Name: CEITEC 2020 (Acronym: CEITEC2020)
LQ1601, research and development project	Investor: Ministry of Education, Youth and Sports of the CR