Informační systém MU
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. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2012, vol. 287, No 6, p. 4335-4347. ISSN 0021-9258. doi:10.1074/jbc.M111.314831.
Other formats:   BibTeX LaTeX RIS
Basic information
Original name Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes
Authors AUDFRAY, Aymeric (250 France), Julie CLAUDINON (276 Germany), Saida ABOUNIT (250 France), Nathalie RUVOEN-CLOUET (250 France), Goran LARSON (752 Sweden), David F SMITH (840 United States of America), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution), Jacques LE PENDU (250 France), Winfried ROEMER (276 Germany), Annabelle VARROT (250 France) and Anne IMBERTY (250 France).
Edition Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2012, 0021-9258.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 4.651
RIV identification code RIV/00216224:14740/12:00057814
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1074/jbc.M111.314831
UT WoS 000300410900064
Keywords in English BLOOD GROUP ANTIGENS; CEPACIA COMPLEX; CYSTIC-FIBROSIS; PSEUDOMONAS-AERUGINOSA; MOLECULAR-BASIS; SP-NOV.; RECOGNITION; INFECTION; CELLS; GLYCOSYLATION
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 16. 11. 2012 13:30.
Abstract
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.
Links
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
GA303/09/1168, research and development projectName: Lektiny z lidských patogenů - struktura, funkce, inženýrství
Investor: Czech Science Foundation, Lectins from human pathogens - structure, function, engineering
Displayed: 25. 6. 2022 01:55