J 2011

Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity

ŠULÁK, Ondřej, Gianluca CIOCI, Emilie LAMEIGNÈRE, Viviane BALLOY, Adam ROUND et. al.

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 9.127

RIV identification code

RIV/00216224:14740/11:00050198

Organization unit

Central European Institute of Technology

DOI

UT WoS

000295409000041

Keywords in English

bacterial lectin;Burkholderia cenocepacia;calcium-dependent bacterial lectins;TNF;inflammation

Tags

Tags

International impact, Reviewed
Změněno: 24/7/2013 11:05, Olga Křížová

Abstract

V originále

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 project
Name: CEITEC - central european institute of technology
GA303/09/1168, research and development project
Name: Lektiny z lidských patogenů - struktura, funkce, inženýrství
Investor: Czech Science Foundation, Lectins from human pathogens - structure, function, engineering
GD301/09/H004, research and development project
Name: Molekulární a strukturní biologie vybraných cytostatik. Od mechanistických studií k chemoterapii rakoviny
Investor: Czech Science Foundation
LC06030, research and development project
Name: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
ME08008, research and development project
Name: 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 MU
Name: 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