Characterization of novel lectin PLL3 from Photorhabdus
laumondii with a seven bladed beta propeller monomeric
structure

k 2019

Characterization of novel lectin PLL3 from Photorhabdus laumondii with a seven bladed beta propeller monomeric structure

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

Základní údaje

Originální název

Characterization of novel lectin PLL3 from Photorhabdus laumondii with a seven bladed beta propeller monomeric structure

Autoři

FALTINEK, Lukáš (203 Česká republika, domácí), Eva FUJDIAROVÁ (203 Česká republika, domácí), Filip MELICHER (703 Slovensko, domácí), Josef HOUSER (203 Česká republika, domácí) a Michaela WIMMEROVÁ (203 Česká republika, garant, domácí)

Vydání

XX. setkání biochemiků a molekulárních biologů, 2019

Další údaje

Jazyk

angličtina

Typ výsledku

Prezentace na konferencích

Obor

10600 1.6 Biological sciences

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14310/19:00107976

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-80-210-9420-8

Klíčová slova česky

Photorhabdus; lektin; O-methylované sacharidy; L-fukosa; charakterizace proteinů

Klíčová slova anglicky

Photorhabdus; lectin; O-methylated saccharides; L-fucose; protein characterization

Změněno: 28. 11. 2024 15:59, Mgr. Lukáš Faltinek, Ph.D.

Anotace

V originále

Photorhabdus is the genus of Gram-negative bioluminescent bacteria living in the mutualistic relationship with Heterorhabditis nematodes. Photorhabdus and Heterorhabditis form a complex that is highly pathogenic for insects. Focus of research was characterization of recombinant form of lectin PLL3 from P. laumondii subsp. laumondii. PLL3 was discovered to be a novel member of the structural PLL lectin family with seven-bladed beta-propeller fold. Its binding properties were investigated using hemagglutination assay and biophysical methods such as isothermal titration calorimetry and surface plasmon resonance. The structure of PLL3 was solved by X-ray crystallography. Obtained data showed that PLL3 exhibits similar binding properties as the other members of its structural family. PLL3 interacted with L-fucose and its derivatives but was also able to recognize other carbohydrates including O-methylated glycans. O-methylation is unusual glycan modification present in some species of bacteria, fungi, plants and nematodes, but not in insects or mammals. In contrast to previously described PLL family lectins, PLL3 exists as monomer in the solution as well as in the crystal structure. The monomeric state of PLL3 might be responsible for the presence of a weaker avidity effect compared to related lectins. Based on the similarity to the other lectins from PLL family and the fact that these lectins interfere with the host innate immune system, we can assume PLL3 might play a role in the interaction of P. laumondii with both nematodes and insects.

Návaznosti

GA18-18964S, projekt VaV

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

Investor: Grantová agentura ČR, Lektiny a jejich úloha v interakci patogen/hostitel a buněčném rozpoznávání

MUNI/A/1575/2018, interní kód MU

Název: Podpora biochemického výzkumu v roce 2019

Investor: Masarykova univerzita, Podpora biochemického výzkumu v roce 2019, DO R. 2020_Kategorie A - Specifický výzkum - Studentské výzkumné projekty

Citovat

FALTINEK, Lukáš, Eva FUJDIAROVÁ, Filip MELICHER, Josef HOUSER a Michaela WIMMEROVÁ. Characterization of novel lectin PLL3 from Photorhabdus laumondii with a seven bladed beta propeller monomeric structure. In XX. setkání biochemiků a molekulárních biologů. 2019. ISBN 978-80-210-9420-8.

@proceedings{1601177,
   author = {Faltinek, Lukáš and Fujdiarová, Eva and Melicher, Filip and Houser, Josef and Wimmerová, Michaela},
   booktitle = {XX. setkání biochemiků a molekulárních biologů},
   keywords = {Photorhabdus; lectin; O-methylated saccharides; L-fucose; protein characterization},
   language = {eng},
   isbn = {978-80-210-9420-8},
   title = {Characterization of novel lectin PLL3 from Photorhabdus laumondii with a seven bladed beta propeller monomeric structure},
   year = {2019}
}

TY  - CONF
ID  - 1601177
AU  - Faltinek, Lukáš - Fujdiarová, Eva - Melicher, Filip - Houser, Josef - Wimmerová, Michaela
PY  - 2019
TI  - Characterization of novel lectin PLL3 from Photorhabdus laumondii with a seven bladed beta propeller monomeric structure
SN  - 9788021094208
KW  - Photorhabdus
KW  - lectin
KW  - O-methylated saccharides
KW  - L-fucose
KW  - protein characterization
N2  - Photorhabdus is the genus of Gram-negative bioluminescent bacteria living in the mutualistic relationship with Heterorhabditis nematodes. Photorhabdus and Heterorhabditis form a complex that is highly pathogenic for insects. Focus of research was characterization of recombinant form of lectin PLL3 from P. laumondii subsp. laumondii. PLL3 was discovered to be a novel member of the structural PLL lectin family with seven-bladed beta-propeller fold. Its binding properties were investigated using hemagglutination assay and biophysical methods such as isothermal titration calorimetry and surface plasmon resonance. The structure of PLL3 was solved by X-ray crystallography. Obtained data showed that PLL3 exhibits similar binding properties as the other members of its structural family. PLL3 interacted with L-fucose and its derivatives but was also able to recognize other carbohydrates including O-methylated glycans. O-methylation is unusual glycan modification present in some species of bacteria, fungi, plants and nematodes, but not in insects or mammals. In contrast to previously described PLL family lectins, PLL3 exists as monomer in the solution as well as in the crystal structure. The monomeric state of PLL3 might be responsible for the presence of a weaker avidity effect compared to related lectins. Based on the similarity to the other lectins from PLL family and the fact that these lectins interfere with the host innate immune system, we can assume 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 a Michaela WIMMEROVÁ. Characterization of novel lectin PLL3 from Photorhabdus laumondii with a seven bladed beta propeller monomeric structure. In \textit{XX. setkání biochemiků a molekulárních biologů}. 2019. ISBN~978-80-210-9420-8.

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