Characterization of monomeric lectin PLL3 from Photorhabdus
laumondii

a 2021

Characterization of monomeric lectin PLL3 from Photorhabdus laumondii

FALTINEK, Lukáš, Eva FUJDIAROVÁ, Filip MELICHER, Josef HOUSER, Michaela WIMMEROVÁ et. al.

Basic information

Original name

Characterization of monomeric lectin PLL3 from Photorhabdus laumondii

Authors

FALTINEK, Lukáš, Eva FUJDIAROVÁ, Filip MELICHER, Josef HOUSER and Michaela WIMMEROVÁ

Edition

XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section, 2021

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10600 1.6 Biological sciences

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

Organization unit

Faculty of Science

ISBN

978-80-907779-1-0

Keywords (in Czech)

Photorhabdus; lektiny; L-fukosa; charakterizace proteinů

Keywords in English

Photorhabdus; lectins; L-fucose; protein characterization

Změněno: 30/1/2022 19:07, prof. RNDr. Michaela Wimmerová, Ph.D.

Abstract

V originále

Photorhabdus laumondii belongs to the genus of Gram-negative bacteria which live in the gut of Heterorhabditis nematodes. Photorhabdus and Heterorhabditis form a mutualistic complex that is highly pathogenic for a variety of insects. P. laumondii produces five structurally related lectins – proteins, that are generally involved in cell signaling and play important role in many physiological as well as pathophysiological processes. Focus of this research was functional and structural characterization of recombinant form of lectin PLL3 from P. laumondii subsp. laumondii. Its structure was solved by X-ray crystallography and it was revealed, that PLL3 is a new member of the PLL lectin family with seven-bladed β propeller fold. In comparison to previously characterised PLL lectins, PLL3 exists as a monomer both in the crystal structure and in the solution. Its activity was evaluated by hemagglutination assay and its inhibition. Binding properties of PLL3 toward saccharide ligands were investigated by biophysical methods such as isothermal titration calorimetry and surface plasmon resonance. PLL3 exhibited affinity toward L-fucose and its derivatives but was also able to interact with O-methylated glycans. These unusually modified glycans are ordinarily present in some species of bacteria, fungi, plants and nematodes, but are missing in insects or mammals. PLL3 is similar to the other lectins from PLL family which can interfere with the host innate immune system. Therefore there is an assumption that also PLL3 might play a role in the interaction of P. laumondii with both nematodes and insects.

Links

GA18-18964S, research and development project

Name: Lektiny a jejich úloha v interakci patogen/hostitel a buněčném rozpoznávání

Investor: Czech Science Foundation

MUNI/A/1604/2020, interní kód MU

Name: Podpora biochemického výzkumu v roce 2021

Investor: Masaryk University

Citovat

FALTINEK, Lukáš, Eva FUJDIAROVÁ, Filip MELICHER, Josef HOUSER and Michaela WIMMEROVÁ. Characterization of monomeric lectin PLL3 from Photorhabdus laumondii. In XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section. 2021. ISBN 978-80-907779-1-0.

@proceedings{1793240,
   author = {Faltinek, Lukáš and Fujdiarová, Eva and Melicher, Filip and Houser, Josef and Wimmerová, Michaela},
   booktitle = {XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section},
   keywords = {Photorhabdus; lectins; L-fucose; protein characterization},
   language = {eng},
   isbn = {978-80-907779-1-0},
   title = {Characterization of monomeric lectin PLL3 from Photorhabdus laumondii},
   year = {2021}
}

TY  - CONF
ID  - 1793240
AU  - Faltinek, Lukáš - Fujdiarová, Eva - Melicher, Filip - Houser, Josef - Wimmerová, Michaela
PY  - 2021
TI  - Characterization of monomeric lectin PLL3 from Photorhabdus laumondii
SN  - 9788090777910
KW  - Photorhabdus
KW  - lectins
KW  - L-fucose
KW  - protein characterization
N2  - Photorhabdus laumondii belongs to the genus of Gram-negative bacteria which live in the gut of Heterorhabditis nematodes. Photorhabdus and Heterorhabditis form a mutualistic complex that is highly pathogenic for a variety of insects. P. laumondii produces five structurally related lectins – proteins, that are generally involved in cell signaling and play important role in many physiological as well as pathophysiological processes. Focus of this research was functional and structural characterization of recombinant form of lectin PLL3 from P. laumondii subsp. laumondii. Its structure was solved by X-ray crystallography and it was revealed, that PLL3 is a new member of the PLL lectin family with seven-bladed β propeller fold. In comparison to previously characterised PLL lectins, PLL3 exists as a monomer both in the crystal structure and in the solution. Its activity was evaluated by hemagglutination assay and its inhibition. Binding properties of PLL3 toward saccharide ligands were investigated by biophysical methods such as isothermal titration calorimetry and surface plasmon resonance. PLL3 exhibited affinity toward L-fucose and its derivatives but was also able to interact with O-methylated glycans. These unusually modified glycans are ordinarily present in some species of bacteria, fungi, plants and nematodes, but are missing in insects or mammals. PLL3 is similar to the other lectins from PLL family which can interfere with the host innate immune system. Therefore there is an assumption that also PLL3 might play a role in the interaction of P. laumondii with both nematodes and insects.
ER  -

FALTINEK, Lukáš, Eva FUJDIAROVÁ, Filip MELICHER, Josef HOUSER and Michaela WIMMEROVÁ. Characterization of monomeric lectin PLL3 from Photorhabdus laumondii. In \textit{XXVI. Annual Congress of Czech and Slovak Societies for Biochemistry and Molecular Biology with cooperation of Austrian and German Biochemical Section}. 2021. ISBN~978-80-907779-1-0.

Detailed Information on Publication Record