D 2003

Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides

SABIN, Charles, Michaela WIMMEROVÁ, Martina BUDOVÁ, Lenka ŠNAJDROVÁ, Catherine GAUTIER et. al.

Basic information

Original name

Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides

Authors

SABIN, Charles (250 France), Michaela WIMMEROVÁ (203 Czech Republic, guarantor), Martina BUDOVÁ (250 France), Lenka ŠNAJDROVÁ (250 France), Catherine GAUTIER (250 France), Jaroslav KOČA (376 Israel), Edward MITCHELL (250 France), Nechama GILBOA-GARBER (376 Israel) and Anne IMBERTY (250 France)

Edition

Grenoble, France, 12th European Carbohydrate Symposium, p. 390-390, 2003

Publisher

CERMAV-CNRS

Other information

Language

English

Type of outcome

Stať ve sborníku

Field of Study

10600 1.6 Biological sciences

Country of publisher

France

Confidentiality degree

není předmětem státního či obchodního tajemství

RIV identification code

RIV/00216224:14310/03:00008865

Organization unit

Faculty of Science

Keywords in English

Pseudomonas aeruginosa; lectin; microcalorimetry; crystal structure; cystic fibrosis

Tags

International impact
Změněno: 15/11/2006 11:39, prof. RNDr. Michaela Wimmerová, Ph.D.

Abstract

V originále

Pseudomonas aeruginosa galactose- and fucose-binding (PA-IL and PA-IIL) lectins contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A and further refined at 1 Ĺ resolution. Additional experiments have been performed in order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Crystals have been obtained for the complex between PA-ILL and b-Me-D-arabinopyranoside and the structure has been solved at 1.8 A resolution. PA-IIL exhibits unusually high specificity to fucose, which can be related to the presence of two calcium ions in the site. Isothermal titration microcalorimetry (ITC) experiments were performed in order to characterize the thermodynamic parameters of the interaction since this method has been proven to be well adapted to the study of protein/carbohydrate interactions. Several monosaccharides differing only by the group at C5 (L-fucose, L-galactose and D-arabinose) were tested, as well as their methyl-glycosides. Calculations of charges distribution were performed using quantum chemistry in order to rationalize the role of calcium ions in the affinity.

Links

LN00A016, research and development project
Name: BIOMOLEKULÁRNÍ CENTRUM
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Center