Novel two - domain superlectin from the human opportunistic
pathogen Bukholderia cenocepacia

D 2009

Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia

ŠULÁK, Ondřej, Monia DELIA, Gianluca CIOCI, Annabelle VARROT, Anne IMBERTY et. al.

Basic information

Original name

Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia

Name in Czech

Nový superlektin z lidského podmíněného patogenu Burkholderia cenocepacia

Authors

ŠULÁK, Ondřej, Monia DELIA, Gianluca CIOCI, Annabelle VARROT, Anne IMBERTY and Michaela WIMMEROVÁ

Edition

Brno, Cukrblik 2009, p. 28-87, 2009

Publisher

Masarykova univerzita

Other information

Language

English

Type of outcome

Stať ve sborníku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

Organization unit

Faculty of Science

ISBN

978-80-210-4831-7

Keywords in English

Superlectin; X ray; Isothermal titration callorimetry; Burkolderia cenocepacia

Abstract

ORIG CZ

V originále

Lectins are known for their ability to agglutinate erythrocytes in vitro. Plant and animal pathogens use these protein-carbohydrate interactions in their strategy for host recognition and invasion. Burkholderia cenocepacia is a Gram-negative bacterium that can be found throughout the environment.Four genes coding protein homologues to the lectin PA-IIL from Pseudomonas aeruginosa have been found in the genome of B. cenocepacia. One of them, BclC, is a 28 kDa protein. Further sequence analysis showed two distinct domains in the protein structure. The C-terminal part coding lectin domain shows partial homology to the PA-IIL lectin, as mentioned above, and the N-terminal part is unknown. Both domains were also cloned separately. The results indicated the unusual binding activity of the protein. The C-terminal domain recognizes D-mannosylated saccharides with high affinity. Interestingly, the N-terminal domain also displays sugar-binding activity with a strong preference for L-fucosylated oligosaccharides, the Lewis type determinants.

In Czech

Hlavním smyslem této studie je snaha porozumět molekulárním mechanismům, zejména protein sacharidovým interakcím, které umožňují patogenní bakterii takto napadat, kolonizovat a ovlivňovat fysiopatologii jejich hostitele. Detailní funkční studie pomocí Surface Plasmon Resonance a mikrokalorimetrických metod umožnily charakterizovat vazebné vlastnosti (afinita, specifita) a termodynamické parametry interakce lektinu s vybranými sacharidy.

Links

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

Citovat

ŠULÁK, Ondřej, Monia DELIA, Gianluca CIOCI, Annabelle VARROT, Anne IMBERTY and Michaela WIMMEROVÁ. Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia. In Cukrblik 2009. Brno: Masarykova univerzita, 2009, p. 28-87. ISBN 978-80-210-4831-7.

@inproceedings{832437,
   author = {Šulák, Ondřej and Delia, Monia and Cioci, Gianluca and Varrot, Annabelle and Imberty, Anne and Wimmerová, Michaela},
   address = {Brno},
   booktitle = {Cukrblik 2009},
   keywords = {Superlectin; X ray; Isothermal titration callorimetry; Burkolderia cenocepacia},
   language = {eng},
   location = {Brno},
   isbn = {978-80-210-4831-7},
   pages = {28-87},
   publisher = {Masarykova univerzita},
   title = {Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia},
   year = {2009}
}

TY  - JOUR
ID  - 832437
AU  - Šulák, Ondřej - Delia, Monia - Cioci, Gianluca - Varrot, Annabelle - Imberty, Anne - Wimmerová, Michaela
PY  - 2009
TI  - Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia
PB  - Masarykova univerzita
CY  - Brno
SN  - 9788021048317
KW  - Superlectin
KW  - X ray
KW  - Isothermal titration callorimetry
KW  - Burkolderia cenocepacia
N2  - Lectins are known for their ability to agglutinate erythrocytes in vitro. Plant and animal pathogens use these protein-carbohydrate interactions in their strategy for host recognition and invasion. Burkholderia cenocepacia is a Gram-negative bacterium that can be found throughout the environment.Four genes coding protein homologues to the lectin PA-IIL from Pseudomonas aeruginosa have been found in the genome of B. cenocepacia. One of them, BclC, is a 28 kDa protein. Further sequence analysis showed two distinct domains in the protein structure. The C-terminal part coding lectin domain shows partial homology to the PA-IIL lectin, as mentioned above, and the N-terminal part is unknown. Both domains were also cloned separately. The results indicated the unusual binding activity of the protein. The C-terminal domain recognizes D-mannosylated saccharides with high affinity. Interestingly, the N-terminal domain also displays sugar-binding activity with a strong preference for L-fucosylated oligosaccharides, the Lewis type determinants.
ER  -

ŠULÁK, Ondřej, Monia DELIA, Gianluca CIOCI, Annabelle VARROT, Anne IMBERTY and Michaela WIMMEROVÁ. Novel two - domain superlectin from the human opportunistic pathogen Bukholderia cenocepacia. In \textit{Cukrblik 2009}. Brno: Masarykova univerzita, 2009, p.~28-87. ISBN~978-80-210-4831-7.

Detailed Information on Publication Record