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.

Basic information

Original name

Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica

Authors

PAULÍKOVÁ, Gita (203 Czech Republic, belonging to the institution), Josef HOUSER (203 Czech Republic, belonging to the institution), Martina KASAKOVA (203 Czech Republic), Beata OROSZOVA (203 Czech Republic), Benedetta BERTOLOTTI (203 Czech Republic), Kamil PARKAN (203 Czech Republic), Jitka MORAVCOVÁ (203 Czech Republic) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.998

RIV identification code

RIV/00216224:14740/19:00107829

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000490702200019

Keywords (in Czech)

lektin PHL; inhibitor; fukosa

Keywords in English

lectin PHL; inhibitor; fucose

Abstract

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.

Links

GA15-17572S, research and development project

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

Investor: Czech Science Foundation

GA18-18964S, research and development project

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

Investor: Czech Science Foundation

90043, large research infrastructures

Name: CIISB

Citovat

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. 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.

@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.

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