2XR4

C-terminal domain of BC2L-C Lectin from Burkholderia cenocepacia

2XR4 の概要

• エントリーDOI: 10.2210/pdb2xr4/pdb
• 関連するPDBエントリー: 2WQ4
• 分子名称: LECTIN, SULFATE ION (3 entities in total)
• 機能のキーワード: sugar binding protein, lung, pathogen
• 由来する生物種: BURKHOLDERIA CENOCEPACIA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25356.07

構造登録者

Sulak, O.,Cioci, G.,Lameignere, E.,Delia, M.,Wimmerova, M.,Imberty, A. (登録日: 2010-09-09, 公開日: 2011-08-03, 最終更新日: 2023-12-20)

主引用文献

Sulak, O.,Cioci, G.,Lameignere, E.,Balloy, V.,Round, A.,Gutsche, I.,Malinovska, L.,Chignard, M.,Kosma, P.,Aubert, D.F.,Marolda, C.L.,Valvano, M.A.,Wimmerova, M.,Imberty, A.
Burkholderia Cenocepacia Bc2L-C is a Super Lectin with Dual Specificity and Proinflammatory Activity.
Plos Pathog., 7:2238-, 2011

PubMed Abstract: 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, which has two distinct domains with unique specificities and biological activities. The N-terminal domain is a novel TNF-α-like fucose-binding 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. The apo form of the C-terminal domain crystallized as a dimer, and calcium and mannose could be docked in the binding site. The whole lectin is hexameric and the overall structure, determined by electron microscopy and small angle X-ray scattering, reveals a flexible arrangement of three mannose/heptose-specific dimers flanked by two fucose-specific TNF-α-like trimers. We propose that BC2L-C binds to the bacterial surface in a mannose/heptose-dependent manner via the C-terminal domain. The TNF-α-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. The unique architecture of this newly recognized superlectin correlates with multiple functions including bacterial cell cross-linking, adhesion to human epithelia, and stimulation of inflammation.

PubMed: 21909279
DOI: 10.1371/JOURNAL.PPAT.1002238

実験手法

X-RAY DIFFRACTION (1.9 Å)