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

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About: Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.plospathogens.org/article/info%3Adoi%2F10.1371%2Fjournal.ppat.1002238
Description	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. 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. (en)
Title	Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity (en)
skos:prefLabel	Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity (en)
skos:notation	RIV/00216224:14740/11:00050198!RIV12-GA0-14740___
http://linked.open...avai/predkladatel	Středoevropský technologický institut
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(ED1.1.00/02.0068), P(GA303/09/1168), P(GD301/09/H004), P(LC06030), P(ME08008), Z(MSM0021622413)
http://linked.open...iv/cisloPeriodika	9
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Šulák, Ondřej Malinovská, Lenka Wimmerová, Michaela
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	188913
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/11:00050198
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	bacterial lectin; Burkholderia cenocepacia; calcium-dependent bacterial lectins; TNF; inflammation (en)
http://linked.open.../riv/klicoveSlovo	inflammation Burkholderia cenocepacia TNF bacterial lectin calcium-dependent bacterial lectins
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[D20459CDB53C]
http://linked.open...i/riv/nazevZdroje	PLoS Pathogens
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	14 (xsd:int)
http://linked.open...vavai/riv/projekt	Central european institute of technology Lectins from human pathogens - structure, function, engineering Molecular and structural biology of selected antitumor drugs. From mechanistic studies to chemotherapy of tumors Biomolecular centre Design of Carbohydrates and Glycomimetics as Antibacterial and Antiviral Drugs
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	7
http://linked.open...iv/tvurceVysledku	Aubert, Daniel F Balloy, Viviane Chignard, Michel Cioci, Gianluca Gutsche, Irina Imberty, Anne Kosma, Paul Lameignère, Emilie Malinovská, Lenka Marolda, Cristina L Round, Adam Valvano, Miguel A Wimmerová, Michaela Šulák, Ondřej
http://linked.open...ain/vavai/riv/wos	000295409000041
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím
issn	1553-7366
number of pages	14 (xsd:int)
http://bibframe.org/vocab/doi	10.1371/journal.ppat.1002238
http://localhost/t...ganizacniJednotka	14740
is http://linked.open...avai/riv/vysledek of	Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity

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