Fucosylated inhibitors of recently identified bangle lectin
from Photorhabdus asymbiotica

J 2019

Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica

PAULÍKOVÁ, Gita; Josef HOUSER; Martina KASAKOVA; Beata OROSZOVA; Benedetta BERTOLOTTI et al.

Základní údaje

Originální název

Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica

Autoři

PAULÍKOVÁ, Gita; Josef HOUSER; Martina KASAKOVA; Beata OROSZOVA; Benedetta BERTOLOTTI; Kamil PARKAN; Jitka MORAVCOVÁ a Michaela WIMMEROVÁ

Vydání

Scientific reports, LONDON, NATURE PUBLISHING GROUP, 2019, 2045-2322

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.998

Kód RIV

RIV/00216224:14740/19:00107829

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1038/s41598-019-51357-9

UT WoS

000490702200019

EID Scopus

2-s2.0-85073519038

Klíčová slova česky

lektin PHL; inhibitor; fukosa

Klíčová slova anglicky

lectin PHL; inhibitor; fucose

Štítky

CF BIC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 10. 2024 15:02, Ing. Martina Blahová

Anotace

V originále

A recently described bangle lectin (PHL) from the bacterium Photorhabdus asymbiotica was identified as a mainly fucose- binding protein that could play an important role in the host-pathogen interaction and in the modulation of host immune response. Structural studies showed that PHL is a homo-dimer that contains up to seven L-fucose-specific binding sites per monomer. For these reasons, potential ligands of the PHL lectin: alpha-L-fucopyranosyl-containing mono-, di-, tetra-, hexa- and dodecavalent ligands were tested. Two types of polyvalent structures were investigated -calix[4]arenes and dendrimers. The shared feature of all these structures was a C-glycosidic bond instead of the more common but physiologically unstable O-glycosidic bond. The inhibition potential of the tested structures was assessed using different techniques - hemagglutination, surface plasmon resonance, isothermal titration calorimetry, and cell cross-linking. All the ligands proved to be better than free L-fucose. The most active hexava lent dendrimer exhibited affinity three orders of magnitude higher than that of standard L-fucose. To determine the binding mode of some ligands, crystal complex PHL/fucosides 2 -4 were prepared and studied using X-ray crystallography. The electron density in complexes proved the presence of the compounds in 6 out of 7 fucose-binding sites.

Návaznosti

GA15-17572S, projekt VaV

Název: Glykoklastry kalix[4]aren/C-oligosacharidy pro studium selektivity interakcí s lektiny

Investor: Grantová agentura ČR, Glykoklastry kalix[4]aren/C-oligosacharidy pro studium selektivity interakcí s lektiny

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

90043, velká výzkumná infrastruktura

Název: CIISB

Citovat

PAULÍKOVÁ, Gita; Josef HOUSER; Martina KASAKOVA; Beata OROSZOVA; Benedetta BERTOLOTTI; Kamil PARKAN; Jitka MORAVCOVÁ a Michaela WIMMEROVÁ. Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica. Scientific reports. LONDON: NATURE PUBLISHING GROUP, 2019, roč. 9, č. 1, s. 14904-14915. ISSN 2045-2322. Dostupné z: https://doi.org/10.1038/s41598-019-51357-9.

@article{1587058,
   author = {Paulíková, Gita and Houser, Josef and Kasakova, Martina and Oroszova, Beata and Bertolotti, Benedetta and Parkan, Kamil and Moravcová, Jitka and Wimmerová, Michaela},
   article_location = {LONDON},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41598-019-51357-9},
   keywords = {lectin PHL; inhibitor; fucose},
   language = {eng},
   issn = {2045-2322},
   journal = {Scientific reports},
   title = {Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica},
   url = {https://www.nature.com/articles/s41598-019-51357-9.pdf},
   volume = {9},
   year = {2019}
}

TY  - JOUR
ID  - 1587058
AU  - Paulíková, Gita - Houser, Josef - Kasakova, Martina - Oroszova, Beata - Bertolotti, Benedetta - Parkan, Kamil - Moravcová, Jitka - Wimmerová, Michaela
PY  - 2019
TI  - Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica
JF  - Scientific reports
VL  - 9
IS  - 1
SP  - 14904-14915
EP  - 14904-14915
PB  - NATURE PUBLISHING GROUP
SN  - 20452322
KW  - lectin PHL
KW  - inhibitor
KW  - fucose
UR  - https://www.nature.com/articles/s41598-019-51357-9.pdf
L2  - https://www.nature.com/articles/s41598-019-51357-9.pdf
N2  - A recently described bangle lectin (PHL) from the bacterium Photorhabdus asymbiotica was identified as a mainly fucose- binding protein that could play an important role in the host-pathogen interaction and in the modulation of host immune response. Structural studies showed that PHL is a homo-dimer that contains up to seven L-fucose-specific binding sites per monomer. For these reasons, potential ligands of the PHL lectin: alpha-L-fucopyranosyl-containing mono-, di-, tetra-, hexa- and dodecavalent ligands were tested. Two types of polyvalent structures were investigated -calix[4]arenes and dendrimers. The shared feature of all these structures was a C-glycosidic bond instead of the more common but physiologically unstable O-glycosidic bond. The inhibition potential of the tested structures was assessed using different techniques - hemagglutination, surface plasmon resonance, isothermal titration calorimetry, and cell cross-linking. All the ligands proved to be better than free L-fucose. The most active hexava lent dendrimer exhibited affinity three orders of magnitude higher than that of standard L-fucose. To determine the binding mode of some ligands, crystal complex PHL/fucosides 2 -4 were prepared and studied using X-ray crystallography. The electron density in complexes proved the presence of the compounds in 6 out of 7 fucose-binding sites.
ER  -

PAULÍKOVÁ, Gita; Josef HOUSER; Martina KASAKOVA; Beata OROSZOVA; Benedetta BERTOLOTTI; Kamil PARKAN; Jitka MORAVCOVÁ a Michaela WIMMEROVÁ. Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica. \textit{Scientific reports}. LONDON: NATURE PUBLISHING GROUP, 2019, roč.~9, č.~1, s.~14904-14915. ISSN~2045-2322. Dostupné z: https://doi.org/10.1038/s41598-019-51357-9.

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