ŠULÁK, Ondřej, Gianluca CIOCI, Monia DELIA, Martina LAHMANN, Annabelle VARROT, Anne IMBERTY and Michaela WIMMEROVÁ. A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens. Structure. CAMBRIDGE: CELL PRESS, 2010, vol. 18, No 1, p. 59-72. ISSN 0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2009.10.021.
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Basic information
Original name A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
Name in Czech A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
Authors ŠULÁK, Ondřej (203 Czech Republic, belonging to the institution), Gianluca CIOCI (250 France), Monia DELIA (380 Italy, belonging to the institution), Martina LAHMANN (826 United Kingdom of Great Britain and Northern Ireland), Annabelle VARROT (250 France), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution).
Edition Structure, CAMBRIDGE, CELL PRESS, 2010, 0969-2126.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10404 Polymer science
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 6.337
RIV identification code RIV/00216224:14310/10:00057175
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1016/j.str.2009.10.021
UT WoS 000273859700010
Keywords (in Czech) lektin; Burkholderia cenocepacia; patogen; TNF
Keywords in English lectin; Burkholderia cenocepacia; pathogen; TNF
Tags AKR, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 31/10/2012 10:38.
Abstract
The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.
Abstract (in Czech)
Podmíněný patogen Burkholderia cenocepacia produkuje několik rozpustných lektinů. Trimerní N-terminální doména BC2L-C-nt podobná TNF z podmíněného patogenu Burkholderia cenocepacia vykazuje specifitu vůči fukosylovaným lidským krevním antigenům.
Links
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
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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