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

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

Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Biological Chemistry
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://www.jbc.org/content/287/6/4335
Doi http://dx.doi.org/10.1074/jbc.M111.314831
Obor Biochemie
Klíčová slova BLOOD GROUP ANTIGENS; CEPACIA COMPLEX; CYSTIC-FIBROSIS; PSEUDOMONAS-AERUGINOSA; MOLECULAR-BASIS; SP-NOV.; RECOGNITION; INFECTION; CELLS; GLYCOSYLATION
Přiložené soubory
Popis 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.
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