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 (203 Česká republika, domácí), Josef HOUSER (203 Česká republika, domácí), Martina KASAKOVA (203 Česká republika), Beata OROSZOVA (203 Česká republika), Benedetta BERTOLOTTI (203 Česká republika), Kamil PARKAN (203 Česká republika), Jitka MORAVCOVÁ (203 Česká republika) a Michaela WIMMEROVÁ (203 Česká republika, garant, domácí)

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

http://dx.doi.org/10.1038/s41598-019-51357-9

UT WoS

000490702200019

Klíčová slova česky

lektin PHL; inhibitor; fukosa

Klíčová slova anglicky

lectin PHL; inhibitor; fucose

Štítky

CF BIC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 17. 10. 2024 14:05, Ing. Marie Švancarová

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

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

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://dx.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 = {http://dx.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://dx.doi.org/10.1038/s41598-019-51357-9.

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