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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 and 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, vol.~287, No~6, p.~4335-4347. ISSN~0021-9258. Available from: https://dx.doi.org/10.1074/jbc.M111.314831.
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