Structural Basis of the Preferential Binding for Globo-Series
Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I

J 2008

Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I

BLANCHARD, Bertrand, Alessandra NURISSO, Emilie HOLLWILLE, Cecile TETAUD, Joele WIELLS et. al.

Basic information

Original name

Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I

Name in Czech

Strukturní základ vazebných preferencí lektinu I z Pseudomonas aeruginosa vůči glykosfingolipidům Globo-serie

Authors

BLANCHARD, Bertrand (250 France), Alessandra NURISSO (380 Italy), Emilie HOLLWILLE (250 France), Cecile TETAUD (50 Bangladesh), Joele WIELLS (250 France), Martina POKORNÁ (203 Czech Republic), Michaela WIMMEROVÁ (203 Czech Republic, guarantor), Annabelle VARROTTE (250 France) and Anne IMBERTY (250 France)

Edition

Journal of Molecular Biology, Amsterdam, Elsevier, 2008, 0022-2836

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10610 Biophysics

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 4.146

RIV identification code

RIV/00216224:14310/08:00026609

Organization unit

Faculty of Science

UT WoS

000260533800009

Keywords in English

pseudomonas aeruginosa; lectin; molecular modeling; structure;glycosphinglipid; oligosaccharides

Abstract

ORIG CZ

V originále

The opportunistic pathogen Pseudomonas aeruginosa contains several carbohydrate-binding proteins, among which is the P. aeruginosa lectin I (PA-IL), which displays affinity for a-galactosylated glycans. Glycan arrays were screened and demonstrated stronger binding of PA-IL toward aGal1-4bGal-terminating structures and weaker binding to aGal1-3bGal ones in order to determine which human glycoconjugates could play a role in the carbohydrate-mediated adhesion of the bacteria. This was confirmed in vivo by testing the binding of the lectin to Burkitt lymphoma cells that present large amounts of globotriaosylceramide antigen Gb3/CD77/Pk. Trisaccharide moieties of Gb3 and isoglobotriaosylceramide were tested by titration microcalorimetry, and both displayed similar affinity to PA-IL in solution.

In Czech

Strukturní základ vazebných preferencí lektinu I z Pseudomonas aeruginosa vůči glykosfingolipidům Globo-serie

Links

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Citovat

BLANCHARD, Bertrand, Alessandra NURISSO, Emilie HOLLWILLE, Cecile TETAUD, Joele WIELLS, Martina POKORNÁ, Michaela WIMMEROVÁ, Annabelle VARROTTE and Anne IMBERTY. Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I. Journal of Molecular Biology. Amsterdam: Elsevier, 2008, vol. 383, No 4, p. 837-853. ISSN 0022-2836.

@article{787074,
   author = {Blanchard, Bertrand and Nurisso, Alessandra and Hollwille, Emilie and Tetaud, Cecile and Wiells, Joele and Pokorná, Martina and Wimmerová, Michaela and Varrotte, Annabelle and Imberty, Anne},
   article_location = {Amsterdam},
   article_number = {4},
   keywords = {pseudomonas aeruginosa; lectin; molecular modeling; structure;glycosphinglipid; oligosaccharides},
   language = {eng},
   issn = {0022-2836},
   journal = {Journal of Molecular Biology},
   title = {Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I},
   volume = {383},
   year = {2008}
}

TY  - JOUR
ID  - 787074
AU  - Blanchard, Bertrand - Nurisso, Alessandra - Hollwille, Emilie - Tetaud, Cecile - Wiells, Joele - Pokorná, Martina - Wimmerová, Michaela - Varrotte, Annabelle - Imberty, Anne
PY  - 2008
TI  - Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I
JF  - Journal of Molecular Biology
VL  - 383
IS  - 4
SP  - 837-853
EP  - 837-853
PB  - Elsevier
SN  - 00222836
KW  - pseudomonas aeruginosa
KW  - lectin
KW  - molecular modeling
KW  - structure;glycosphinglipid
KW  - oligosaccharides
N2  - The opportunistic pathogen Pseudomonas aeruginosa contains several carbohydrate-binding proteins, among which is the P. aeruginosa lectin I (PA-IL), which displays affinity for a-galactosylated glycans. Glycan arrays were screened and demonstrated stronger binding of PA-IL toward aGal1-4bGal-terminating structures and weaker binding to aGal1-3bGal ones in order to determine which human glycoconjugates could play a role in the carbohydrate-mediated adhesion of the bacteria. This was confirmed in vivo by testing the binding of the lectin to Burkitt lymphoma cells that present large amounts of globotriaosylceramide antigen Gb3/CD77/Pk. Trisaccharide moieties of Gb3 and isoglobotriaosylceramide were tested by titration microcalorimetry, and both displayed similar affinity to PA-IL in solution.
ER  -

BLANCHARD, Bertrand, Alessandra NURISSO, Emilie HOLLWILLE, Cecile TETAUD, Joele WIELLS, Martina POKORNÁ, Michaela WIMMEROVÁ, Annabelle VARROTTE and Anne IMBERTY. Structural Basis of the Preferential Binding for Globo-Series Glycosphingolipids Displayed by Pseudomonas aeruginosa Lectin I. \textit{Journal of Molecular Biology}. Amsterdam: Elsevier, 2008, vol.~383, No~4, p.~837-853. ISSN~0022-2836.

Detailed Information on Publication Record