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@article{1073535, author = {Audfray, Aymeric and Claudinon, Julie and Abounit, Saida and RuvoenandClouet, Nathalie and Larson, Goran and Smith, David F and Wimmerová, Michaela and Le Pendu, Jacques and Roemer, Winfried and Varrot, Annabelle and Imberty, Anne}, article_location = {Bethesda, USA}, article_number = {6}, doi = {http://dx.doi.org/10.1074/jbc.M111.314831}, keywords = {BLOOD GROUP ANTIGENS; CEPACIA COMPLEX; CYSTIC-FIBROSIS; PSEUDOMONAS-AERUGINOSA; MOLECULAR-BASIS; SP-NOV.; RECOGNITION; INFECTION; CELLS; GLYCOSYLATION}, language = {eng}, issn = {0021-9258}, journal = {Journal of Biological Chemistry}, title = {Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes}, url = {http://www.jbc.org/content/287/6/4335}, volume = {287}, year = {2012} }
TY - JOUR ID - 1073535 AU - 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 PY - 2012 TI - Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes JF - Journal of Biological Chemistry VL - 287 IS - 6 SP - 4335-4347 EP - 4335-4347 PB - Amer. Soc. Biochem. Mol. Biol. SN - 00219258 KW - BLOOD GROUP ANTIGENS KW - CEPACIA COMPLEX KW - CYSTIC-FIBROSIS KW - PSEUDOMONAS-AERUGINOSA KW - MOLECULAR-BASIS KW - SP-NOV. KW - RECOGNITION KW - INFECTION KW - CELLS KW - GLYCOSYLATION UR - http://www.jbc.org/content/287/6/4335 L2 - http://www.jbc.org/content/287/6/4335 N2 - 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. ER -
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. Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2012, roč.~287, č.~6, s.~4335-4347. ISSN~0021-9258. Dostupné z: https://dx.doi.org/10.1074/jbc.M111.314831.
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