ŠULÁK, Ondřej, Monia DELIA, Nikola KOSTLÁNOVÁ, Anne IMBERTY and Michaela WIMMEROVÁ. CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA. In XII. Setkání biochemiků a molekulárních biologů. Brno: Masarykova univerzita, 2008, p. 53-54. ISBN 978-80-210-4526-2.
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Basic information
Original name CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA
Name in Czech Charakterizace nového lektinu BclC z lidského podmíněného patogenu B. Cenocepacia
Authors ŠULÁK, Ondřej (203 Czech Republic, guarantor), Monia DELIA (380 Italy), Nikola KOSTLÁNOVÁ (203 Czech Republic), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic).
Edition Brno, XII. Setkání biochemiků a molekulárních biologů, p. 53-54, 2 pp. 2008.
Publisher Masarykova univerzita
Other information
Original language English
Type of outcome Proceedings paper
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/08:00024871
Organization unit Faculty of Science
ISBN 978-80-210-4526-2
Keywords in English Lectin; Burkholderia cenocepacia; SPR; ITC
Tags Burkholderia cenocepacia, ITC, lectin, SPR
Tags International impact
Changed by Changed by: Mgr. Ondřej Šulák, Ph.D., učo 54790. Changed: 20/5/2009 17:04.
Abstract
Four genes coding proteins homologous to lectin PA-IIL from Pseudomonas aeruginasa have been found in the genome of B. cenocepacia. One of them, named BclC, is a 28 kDa protein which is able to recognize D-mannosylated carbohydrates. This protein also exhibits partial sequence homology with the protein CV-IIL from the Chromobacterium violaceum. BclC has been cloned and prepared in recombinant form. Sequence analysis showed two distinct domains in the protein, N-terminal part that does not have any sequence homolog in genomic and protein databases, and C-terminal part that codes for lectin domain. Both domains were also cloned separately to simplify further structure-function characterization. Detailed functional studies using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters.
Abstract (in Czech)
Four genes coding proteins homologous to lectin PA-IIL from Pseudomonas aeruginasa have been found in the genome of B. cenocepacia. One of them, named BclC, is a 28 kDa protein which is able to recognize D-mannosylated carbohydrates. This protein also exhibits partial sequence homology with the protein CV-IIL from the Chromobacterium violaceum. BclC has been cloned and prepared in recombinant form. Sequence analysis showed two distinct domains in the protein, N-terminal part that does not have any sequence homolog in genomic and protein databases, and C-terminal part that codes for lectin domain. Both domains were also cloned separately to simplify further structure-function characterization. Detailed functional studies using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters.
Links
GA303/06/0570, research and development projectName: Strukturně-funkční studie lektinů a adhezinů patogenních mikroorganismů
Investor: Czech Science Foundation, Structure-function studies on lectins and adhesins from microbial patogens
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
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