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@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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