ŠULÁK, Ondřej, Gianluca CIOCI, Emilie LAMEIGNÈRE, Viviane BALLOY, Adam ROUND, Irina GUTSCHE, Lenka MALINOVSKÁ, Michel CHIGNARD, Paul KOSMA, Daniel F AUBERT, Cristina L MAROLDA, Miguel A VALVANO, Michaela WIMMEROVÁ and Anne IMBERTY. Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity. PLoS Pathogens. PUBLIC LIBRARY SCIENCE, 2011, vol. 7, No 9, p. "nestránkováno", 14 pp. ISSN 1553-7366. Available from: https://dx.doi.org/10.1371/journal.ppat.1002238.
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Basic information
Original name Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity
Authors ŠULÁK, Ondřej (203 Czech Republic, belonging to the institution), Gianluca CIOCI (250 France), Emilie LAMEIGNÈRE (250 France), Viviane BALLOY (250 France), Adam ROUND (250 France), Irina GUTSCHE (250 France), Lenka MALINOVSKÁ (203 Czech Republic, belonging to the institution), Michel CHIGNARD (250 France), Paul KOSMA (40 Austria), Daniel F AUBERT (124 Canada), Cristina L MAROLDA (124 Canada), Miguel A VALVANO (124 Canada), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution) and Anne IMBERTY (250 France).
Edition PLoS Pathogens, PUBLIC LIBRARY SCIENCE, 2011, 1553-7366.
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: 9.127
RIV identification code RIV/00216224:14740/11:00050198
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1371/journal.ppat.1002238
UT WoS 000295409000041
Keywords in English bacterial lectin;Burkholderia cenocepacia;calcium-dependent bacterial lectins;TNF;inflammation
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 24/7/2013 11:05.
Abstract
Lectins and adhesins are involved in bacterial adhesion to host tissues and mucus during early steps of infection. We report the characterization of BC2L-C, a soluble lectin from the opportunistic pathogen Burkholderia cenocepacia. The N-terminal domain is a novel TNF-a-like fucosebinding lectin, while the C-terminal part is similar to a superfamily of calcium-dependent bacterial lectins. The C-terminal domain displays specificity for mannose and L-glycero-D-manno-heptose. BC2L-C is therefore a superlectin that binds independently to mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes. We propose that BC2L-C binds to the bacterial surface in a mannose/heptose-dependent manner via the C-terminal domain. The TNF-a-like domain triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner, and is therefore proposed to play a role in the dysregulated proinflammatory response observed in B. cenocepacia lung infections.
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
GD301/09/H004, research and development projectName: Molekulární a strukturní biologie vybraných cytostatik. Od mechanistických studií k chemoterapii rakoviny
Investor: Czech Science Foundation
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
ME08008, research and development projectName: Návrh antibakteriálních a antivirových léků na bázi cukrů a glykomimetik
Investor: Ministry of Education, Youth and Sports of the CR, Design of Carbohydrates and Glycomimetics as Antibacterial and Antiviral Drugs, Research and Development Programme KONTAKT (ME)
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
205872, interní kód MUName: Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions (Acronym: POSTBIOMIN)
Investor: European Union, Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions, Capacities
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