Other formats:
BibTeX
LaTeX
RIS
@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 and Michaela WIMMEROVÁ. Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica. \textit{Scientific reports}. LONDON: NATURE PUBLISHING GROUP, 2019, vol.~9, No~1, p.~14904-14915. ISSN~2045-2322. Available from: https://dx.doi.org/10.1038/s41598-019-51357-9.
|
