J 2012

Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes

AUDFRAY, Aymeric; Julie CLAUDINON; Saida ABOUNIT; Nathalie RUVOEN-CLOUET; Goran LARSON et al.

Základní údaje

Originální název

Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes

Autoři

AUDFRAY, Aymeric; Julie CLAUDINON; Saida ABOUNIT; Nathalie RUVOEN-CLOUET; Goran LARSON; David F SMITH; Michaela WIMMEROVÁ; Jacques LE PENDU; Winfried ROEMER; Annabelle VARROT a Anne IMBERTY

Vydání

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2012, 0021-9258

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 4.651

Kód RIV

RIV/00216224:14740/12:00057814

Organizační jednotka

Středoevropský technologický institut

UT WoS

000300410900064

Klíčová slova anglicky

BLOOD GROUP ANTIGENS; CEPACIA COMPLEX; CYSTIC-FIBROSIS; PSEUDOMONAS-AERUGINOSA; MOLECULAR-BASIS; SP-NOV.; RECOGNITION; INFECTION; CELLS; GLYCOSYLATION

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 16. 11. 2012 13:30, Olga Křížová

Anotace

V originále

Burkholderia ambifaria is generally associated with the rhizosphere of plants where it has biocontrol effects on other microorganisms. It is also a member of the Burkholderia cepacia complex, a group of closely related bacteria that cause lung infections in immunocompromised patients as well as in patients with granulomatous disease or cystic fibrosis. Our previous work indicated that fucose on human epithelia is a frequent target for lectins and adhesins of lung pathogens (Sulak, O., Cioci, G., Lameignere, E., Balloy, V., Round, A., Gutsche, I., Malinovska, L., Chignard, M., Kosma, P., Aubert, D. F., Marolda, C. L., Valvano, M. A., Wimmerova, M., and Imberty, A. (2011) PLoS Pathog. 7, e1002238). Analysis of the B. ambifaria genome identified BambL as a putative fucose-binding lectin. The 87-amino acid protein was produced recombinantly and demonstrated to bind to fucosylated oligosaccharides with a preference for alpha Fuc1-2Gal epitopes. Crystal structures revealed that it associates as a trimer with two fucose-binding sites per monomer. The overall fold is a six-bladed beta-propeller formed by oligomerization as in the Ralstonia solanacearum lectin and not by sequential domains like the fungal fucose lectin from Aleuria aurantia. The affinity of BambL for small fucosylated glycans is very high as demonstrated by microcalorimetry (K-D < 1 mu M). Plant cell wall oligosaccharides and human histo-blood group oligosaccharides H-type 2 and Lewis Y are bound with equivalent efficiency. Binding to artificial glycosphingolipid-containing vesicles, human saliva, and lung tissues confirmed that BambL could recognize a wide spectrum of fucosylated epitopes, albeit with a lower affinity for biological material from nonsecretor individuals.

Návaznosti

ED1.1.00/02.0068, projekt VaV
Název: CEITEC - central european institute of technology
GA303/09/1168, projekt VaV
Název: Lektiny z lidských patogenů - struktura, funkce, inženýrství
Investor: Grantová agentura ČR, Lektidy z lidských patogenů - struktura, funkce, inženýrství

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