2012
Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide
MARCHETTI, Roberta; Lenka MALINOVSKÁ; Emilie LAMEIGNERE; Lenka ADAMOVÁ; Cristina DE CASTRO et al.Základní údaje
Originální název
Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide
Autoři
MARCHETTI, Roberta; Lenka MALINOVSKÁ ORCID; Emilie LAMEIGNERE; Lenka ADAMOVÁ; Cristina DE CASTRO; Gianluca CIOCI; Christian STANETTY; Paul KOSMA; Antonio MOLINARO; Michaela WIMMEROVÁ; Anne IMBERTY a Alba SILIPO
Vydání
Glycobiology, Oxford, Oxford University Press, 2012, 0959-6658
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 3.537
Kód RIV
RIV/00216224:14740/12:00057548
Organizační jednotka
Středoevropský technologický institut
UT WoS
000308011800011
Klíčová slova anglicky
bacterial lectin;heptose;lipopolysaccharide;NMR;titration microcalorimetry
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 6. 4. 2013 21:20, Olga Křížová
Anotace
V originále
Bacteria from the Burkholderia cepacia complex (Bcc) cause highly contagious pneumonia among cystic fibrosis (CF) patients. Among them, Burkholderia cenocepacia is one of the most dangerous in the Bcc and is the most frequent cause of morbidity and mortality in CF patients. Indeed, it is responsible of “cepacia syndrome”, a deadly exacerbation of infection, that is the main cause of poor outcomes in lung transplantation. Burkholderia cenocepacia produces several soluble lectins with specificity for fucosylated and mannosylated glycoconjugates. These lectins are present on the bacterial cell surface and it has been proposed that they bind to lipopolysaccharide epitopes. In this work, we report on the interaction of one B. cenocepacia lectin, BC2L-A, with heptose and other manno configured sugar residues. Saturation transfer difference NMR spectroscopy studies of BC2L-A with different mono- and disaccharides demonstrated the requirement of manno configuration with the hydroxyl or glycol group at C6 for the binding process. The crystal structure of BC2L-A complexed with the methyl-heptoside confirmed the location of the carbohydrate ring in the binding site and elucidated the orientation of the glycol tail, in agreement with NMR data. Titration calorimetry performed on monosaccharides, heptose disaccharides and bacterial heptose-containing oligosaccharides and polysaccharides confirmed that bacterial cell wall contains carbohydrate epitopes that can bind to BC2L-A. Additionally, the specific binding of fluorescent BC2L-A lectin on B. cenocepacia bacterial surface was demonstrated by microscopy.
Návaznosti
| ED1.1.00/02.0068, projekt VaV |
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| GA303/09/1168, projekt VaV |
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| GD301/09/H004, projekt VaV |
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